University of Dundee, Scotland, United Kingdom invites online Application for number of Fully Funded PhD Degree at various Departments. We are providing a list of Fully Funded PhD Programs available at University of Dundee, Scotland, United Kingdom.
Eligible candidate may Apply as soon as possible.
(01) PhD Degree – Fully Funded
PhD position summary/title: New technologies to monitor assembly of alternative forms of the proteasome
The PhD project aims to engineer the proteasome and develop new technologies to monitor the assembly of its alternative forms, in a format suitable for high-throughput screening. These tools will be instrumental in uncovering the functions of alternative proteasome complexes and in clarifying their involvement in disease. For example, mutations in proteasome subunits cause proteasomopathies (juvenile neurodevelopmental disorders), while mutations in proteasome-associated proteins are linked to early-onset Parkinson’s disease. Ultimately, this work will lay the foundation for novel strategies to restore protein homeostasis in neurodegenerative disorders. The project will offer training opportunities in state-of-the-art technologies such as cell engineering (CRISPR-Cas9 gene editing of proteasome genes), molecular biology (proteasome and protein degradation assays), and high-resolution confocal microscopy (proteasome dynamics).
Deadline : 31 October 2025
(02) PhD Degree – Fully Funded
PhD position summary/title: Crosstalk between UPR Signaling and ER-phagy during ER Stress
The endoplasmic reticulum (ER) plays a central role in protein folding, modification, and secretion. Perturbations in these processes trigger ER stress and activate the unfolded protein response (UPR), a signaling network that aims to restore ER homeostasis. Dysregulation of ER homeostasis contributes to a wide range of pathologies, including cancer, tissue fibrosis, metabolic disorders, and neurodevelopmental defects. ER quality control is also maintained by the proteasome (via ER-associated degradation, ERAD) and the autolysosome (via ER-specific autophagy, ER-phagy)1-3. Together, the UPR, ERAD, and ER-phagy coordinate ER quality control to safeguard cellular function.
Whereas the UPR is canonically known to activate ERAD, our recent unpublished data indicate that UPR signaling represses ER-phagy activity. This observation has strong implications for autoimmune diseases such as systemic lupus erythematosus and rheumatoid arthritis, where antibody hyperproduction drives chronic ER stress and aberrant UPR activation. We hypothesize that the UPR–ER-phagy axis could represent a therapeutic target, enabling rerouting of excess antibody cargo towards autophagic degradation rather than secretion.
The aim of this PhD project is to elucidate the molecular mechanisms by which UPR signaling regulates ER-phagy and to investigate the physiological relevance of this crosstalk in autoimmune disease models. The project will employ disease-relevant immune cell systems to explore the feasibility of activating ER-phagy to promote degradation of ER proteins, including misfolded aggregates and antibodies.
Deadline : 31 October 2025
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(03) PhD Degree – Fully Funded
PhD position summary/title: Cleave to Modify: A new biological mechanism for protein regulation
This PhD project aims to identify novel substrates and pathways regulated by the “cleave-to-modify” mechanism and link these discoveries to cellular function. By doing so, the project will provide fundamental insights into how proteolytic processing diversifies protein function and reveal new opportunities for therapeutic intervention.
This project takes advantage of our recently developed toolkit to study UBL fusion proteins and their processing4. Students interested in gaining expertise in a wide variety of approaches are strongly encouraged to apply, since the project merges several disciplines, including: method development, state-of-the-art mass spectrometry, cell biology, biophysics, and biochemistry.
Deadline : 31 October 2025
(04) PhD Degree – Fully Funded
PhD position summary/title: Decoding a New Signalling Axis in Parkinson’s Disease
You will investigate how disrupting the TMEM55B–RILPL1 axis impacts lysosomal biology and Parkinson’s disease -relevant signalling. Using brain tissue and primary cells from these mouse models, you will perform lysosome immunoprecipitations (Lyso-IPs) followed by deep proteomic, lipidomic, and phosphoproteomic profiling using advanced mass spectrometry. You will analyse multi-omics datasets to map signalling changes, identify key effectors, and validate them through mechanistic cell biology experiments.
Deadline : 31 October 2025
(05) PhD Degree – Fully Funded
PhD position summary/title: From Data to Biology: AI-Driven Biomarker Discovery and Validation in Parkinson’s Disease through the MJFF LITE Initiative
In this project, emerging AI technologies such as unsupervised learning and computational and experimental approaches will be combined to interrogate the LITE datasets, integrating genetics, large scale mass-spectrometry datasets and clinical phenotyping to identify wet biomarker signatures of LRRK2 driven biology. Identified biomarker signatures in LRRK2 mutation carriers will then be extended to idiopathic PD, with the aim of stratifying patients who might benefit from LRRK2-targeted therapies.
Computational discoveries will be validated experimentally in the laboratory using patient-derived samples and model systems. Approaches will include CRISPR–Cas9 genome editing, knock-in mouse models, immunoblotting, cell-based assays, and ultra-sensitive mass spectrometry, linking computational predictions to biological mechanisms.
Deadline : 31 October 2025
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(06) PhD Degree – Fully Funded
PhD position summary/title: Decoding the mechanism and function of ER-Ribosome associated Quality Control
Approximately one third of the human proteome depends on the endoplasmic reticulum (ER) for its biosynthesis. During translation, ribosomes can sometimes stall, triggering a chain of events that results in the decay of defective mRNAs, recycling of stalled ribosomes and crucially, degradation of partially synthesized nascent polypeptides. UFM1 is an enigmatic ubiquitin-like modifier that is attached to ER-associated ribosomes when stalling occurs. The role of this UFM1 attachment is not fully understood, but mutations in the UFM1 pathway have been found in several neurodevelopmental disorders, emphasizing its significance.
The goal of this project is to define how ribosomes get UFMylated upon stalling and to investigate the mechanisms and function of ribosome UFMylation. This project will build on our recent unpublished work, and we are looking for curious and creative students to work at the frontier of an exciting new field. What makes this project especially exciting is its potential to reveal a fundamental pathway responsible for quality control and homeostasis at the ER, the disruption of which causes disease.
Deadline : 31 October 2025
(07) PhD Degree – Fully Funded
PhD position summary/title: Decoding the hidden language of ubiquitin: non-canonical ubiquitylation in human health and disease
Ubiquitylation is one of the cell’s most powerful control switches, fine-tuning everything, from protein stability to gene expression. When this system malfunctions, it fuels diseases including cancer, neurodegeneration and immunity disorders. This PhD project will focus on exploring non-canonical ubiquitylation – a paradigm-shifting discovery where ubiquitin tags not just lysine residues on proteins but also serine, threonine, DNA, RNA, and sugars. Decoding this hidden molecular “language” of ubiquitin could transform our understanding of cell regulation and uncover untapped therapeutic possibilities.
Recent work in the De Cesare lab has identified the UBE2Q family of ubiquitin-conjugating enzymes (UBE2Q1, UBE2Q2, and UBE2QL1) as key mediators of non-canonical ubiquitylation[1]. These enzymes are linked to vital processes such as lysophagy and embryo implantation and are dysregulated in cancer and neuronal apoptosis – pointing to a widespread but hidden role in human health and disease.
Deadline : 31 October 2025
(08) PhD Degree – Fully Funded
PhD position summary/title: Structural and Chemical Biology of Ubiquitin E3 Ligases
The covalent attachment of the small protein ubiquitin to substrates regulates virtually all cellular processes, and its modulation with small molecules is poised to revolutionise modern medicine. Central to the ubiquitin system are E3 ligase enzymes, which catalyse the covalent transfer of ubiquitin to specific substrates.
Our multidisciplinary lab has developed pioneering technologies for E3 ligase discovery and activity measurement 1,2. Using these approaches, we have identified several E3 ligases with unconventional transfer and regulatory mechanisms 2-5. For example, MYCBP2, a member of the RING-Cys-relay (RCR) subtype, is a central regulator of neuronal integrity 2,3. We have also characterised RNF213-ZNFX1 (RZ-type) E3 ligases, which confer innate restriction to microbial pathogens. Their distinct ubiquitin transfer mechanisms and remarkable regulatory interplay with nucleotide- and nucleic acid–binding domains unlocks novel ways of therapeutically modulating E3 activity.
Deadline : 31 October 2025
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(09) PhD Degree – Fully Funded
PhD position summary/title: Unravelling the molecular mechanisms of amyotrophic lateral sclerosis/motor neuron disease
Amyotrophic lateral sclerosis (ALS)—the commonest type of motor neuron disease (MND)—is a rapidly progressive paralysing illness of mid-adulthood. It has a lifetime risk of ~1 in 400, resulting from the selective neurodegeneration of upper and lower motor neurons (MNs). ~10% of ALS is inherited, and the rest occurs spontaneously. The median survival from symptom onset is 3 years and there are no significant treatments, and no cure. The only globally licensed medication, Riluzole, prolongs survival by a few months on average, and was introduced in the mid 1990s. Consequently, there is a major impetus to unravel the key molecular pathomechanisms to make a breakthrough.
To date, mutations in >40 genes have been identified as a cause of familial ALS/MND that have significantly advanced our understanding of the pathogenesis. Several encode or could interact with protein kinases, implicating dysregulation of protein phosphorylation in ALS pathogenesis, although a single coherent signalling pathway that explains MN degeneration remains elusive.
Deadline : 31 October 2025
(10) PhD Degree – Fully Funded
PhD position summary/title: Deciphering novel ALS signalling pathways: Biomarker discovery and developing therapeutic strategies
Motor neuron disease also referred as Amyotrophic lateral sclerosis (ALS) is a rapidly progressive debilitating disease affecting upper and lower motor neurons with a median survival rate of 2-3 years. Currently, riluzole that extends survival by only 2-3 months, is the only globally approved drug. The well studied ALS genes include TDP-43, an RNA-binding protein localised within nucleus that regulate splicing and RNA metabolism. Loss of function (LoF) of TDP-43 leads nuclear mis-localisation and cytoplasmic aggregation which is a hallmark of 97% of ALS cases and indeed observed in other neurogenerative diseases such as FTD and Alzheimer’s. LoF TDP-43 leads to the generation of several cryptic exons on plethora of genes and have been observed to be denovo translated leading to non-functional protein products and may affect their natural function and altered signalling cascades (1). There is an unmet need to better understand the pathways and molecular consequences of loss of function (LoF) and gain of toxicity of TDP-43 in neuronal and glial cells which collectively has been implicated as a key feature of TDP-43 proteinopathies.
A PhD project is available to develop a knowledgebase of TDP-43 loss of function (LoF) mediated cryptic splicing, identification of cryptic peptides, development of ultra-sensitive assays for mechanistic understanding TDP-43 LoF biology.
Deadline : 31 October 2025
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(11) PhD Degree – Fully Funded
PhD position summary/title: Discovery of novel organelle and ubiquitin mechanisms underlying Parkinson’s disease
Parkinson’s disease (PD) is a movement disorder that is now the fastest growing neurological disorder in the world. Despite much research the disease is incurable and there are no treatments that can slow the disease down. The discovery of genetic mutations in rare familial forms has transformed our understanding of the origins of PD but the function of these genes is poorly understood. Mutations in PTEN-induced kinase 1 (PINK1) cause autosomal recessive PD. PINK1 is unique amongst all protein kinases due to the presence of a mitochondrial targeting domain that localises it to mitochondria. Our lab has made a number of groundbreaking discoveries and uncovered mechanisms that explain how PINK1 and Parkin activation lead to the removal of damaged mitochondria by mitophagy. Excitingly based on this research there are now Phase I trials for PD patients using molecules that boost PINK1-dependent mitophagy. However, there remain many outstanding questions on the regulation of PINK1 and its downstream biology that may lead to new diagnostic and therapeutic strategies to tackle PD. These include the molecular mechanism by which PINK1 senses mitochondrial damage; the role of other PINK1 substrates including Rab GTPases; how PINK1 mutations impacts other organelles including lysosomes and endosomes;; and identification of ubiquitin regulators of PINK1 dependent mechanisms. Our lab uses a multidisciplinary approach to address these questions and the successful student will gain exposure and training in many state-of-the-art methods including mass spectrometry / proteomic technologies; CRISPR/Cas9 technologies; cutting edge methods to isolate organelles, and tissue culture using human iPSC-derived neurons or mice-based analysis. The lab also collaborates with many labs around the world and is actively involved in public engagement. In addition to training and development opportunities within the MRC Protein Phosphorylation & Ubiquitylation Unit and Dundee , the Muqit lab is a member of the EMBO Young Investigator Network (https://people.embo.org/profile/miratul-muqit) and students have opportunities to attend EMBO PhD courses and workshops. The lab is also part of the innovative global Aligning Science Across Parkinson’s (ASAP) initiative (https://parkinsonsroadmap.org) that also enables students to experience cutting edge development opportunities.
Deadline : 31 October 2025
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(12) PhD Degree – Fully Funded
PhD position summary/title: Destroying cancer-causing proteins
This PhD project will explore precisely how FAM83D, FAM83F, and FAM83G regulate cell division and cancer cell proliferation, with a particular focus on their degradation as a therapeutic strategy. The project will employ a wide range of multi-disciplinary cutting-edge technologies, such as CRISPR/Cas9 genome editing, mass-spectrometry, DEL screens to identify ligands for FAM83D, FAM83F and FAM83G, and development and application of small molecule degraders, including PROTACs and molecular glues, against FAM83D-CK1-alpha, FAM83F-CK1-alpha and FAM83G-CK1-alpha complexes. The aim is to establish a mechanistic foundation and therapeutic rationale for selectively degrading these proteins complexes to suppress cancer cell growth.
Deadline : 31 October 2025
(13) PhD Degree – Fully Funded
PhD position summary/title: How do Dysregulated Signalling Pathways cause Intellectual Disability?
This PhD project aims to map signalling pathways that are disrupted in intellectual disability, with the overarching goal of uncovering much-needed therapeutic opportunities in this area. The successful candidate will have the opportunity to utilise exciting new tools and reagents in the lab and expand on our recent progress in dissecting intellectual disability signalling networks. Potential approaches include (phospho)proteomic profiling mass-spectrometry, modelling human neural development using pluripotent stem cells, animal models of intellectual disability, cutting edge biochemistry, and structural analysis using Cryogenic Electron Microscopy (CryoEM). The student will be embedded in a dynamic team with a track record in dissecting intellectual disability signalling networks. They will also have excellent opportunities for further internal and external collaborations with leading experts in this area.
Deadline : 31 October 2025
(14) PhD Degree – Fully Funded
PhD position summary/title: Finding the eat-me signals
The Ganley lab is interested in unravelling the molecular mechanism of autophagy (which literally translates from the Greek meaning to eat oneself). Autophagy is a critical lysosomal degradation pathway that functions to clear the cell of potentially damaging agents, such as protein aggregates or faulty mitochondria. Importantly, autophagy appears to be dysregulated in many diseases and therefore its modulation could lead to novel therapies. However, to enable this, we first need to understand the machinery involved.
A project is available to decipher the signals that lead to the specific autophagy of mitochondria (termed mitophagy), a process that has strong links to cancer and in particular Parkinson’s disease. Following up on recently published work, the project will utilise state-of-the-art microscopy, cell biology, protein biochemistry and mass spectrometry to identify phosphorylation and ubiquitylation events involved in capturing mitochondria for degradation. As well as gaining experience in a wide variety of techniques, you will be part of a dynamic and collaborative team intent on making new scientific discoveries and producing the next generation of world-class scientists.
Deadline : 31 October 2025
(15) PhD Degree – Fully Funded
PhD position summary/title: Genome Bodyguards: Investigating the Cell’s Hidden Repair Team
The MMS22L–TONSL complex is a molecular “first responder” that helps cells protect and repair their DNA when it gets damaged during everyday life. In fact, when we use genome-editing to switch off this complex, cells die within one cell division. The problem is that without it, cells struggle to maintain the integrity of their genetic material—a problem at the heart of cancer, ageing, and many inherited diseases. Actually, TONSL overexpression has been linked to a range of cancers, and mutation in this gene cause debilitating symptoms. A major issue this that we don’t know how MMS22L-TONSL works at the molecular level. This state-of-the-art PhD project will explore how this complex works at the molecular level, discovering how it recognizes broken DNA, recruits repair machinery, and safeguards the stability of the genome. The project you’ll be part of is a collaboration with leading experts in genome maintenance around the world. By combining cutting-edge biochemistry, molecular biology, structural studies, and live-cell imaging, as well as genome-editing and genome-wide “-omic” technologies, the project aims to uncover new exciting insights into how cells defend themselves and how these processes can be harnessed in medicine.
Deadline : 31 October 2025
(16) PhD Degree – Fully Funded
PhD position summary/title: Viral interference of ISG15 signals
One of the most important challenges facing biomedical research is to understand the molecular details of how our immune system defends against pathogens. In the Swatek lab, we aim to understand the roles of ubiquitin and ubiquitin-like modifications in the antiviral state (1). These modifications have emerged as crucial mediators of the signal transduction pathways that sense and respond to viruses. The ubiquitin-like protein, ISG15, is highly upregulated during viral infection and marks thousands of proteins to help shape the host defence response. To subvert ISG15 signalling, many viruses encode enzymes that remove these modifications, and we have previously identified an elegant example of viral-mediated ISG15 suppression (2). Surprisingly, however, the roles of the vast majority of ISG15 modifications are unknown, and therefore, understanding how ISG15 contributes to the antiviral state is of paramount importance. This PhD project aims to identify the ISG15 substrates targeted by viral effector proteins and link these discoveries to a cellular function.
This project takes advantage of our expansive toolkit to study the ISG15 system. Students interested in gaining expertise in a wide variety of approaches are strongly encouraged to apply since the project merges several disciplines, including method development, state-of-the-art mass spectrometry, cell biology, structural biology, biophysics, and biochemistry (3-4). The student will have the opportunity to participate in several internal and external collaborations.
Deadline : 31 October 2025
(17) PhD Degree – Fully Funded
PhD position summary/title: Investigating the immune-epithelial interactions that drive intestinal inflammation
Intraepithelial T lymphocytes (IELs) are at the forefront of mucosal immunity – the first immune cells that pathogens and symbionts encounter in the gut. IELs are central to the protection of the gut against infection and dietary stress, but dysregulated IELs responses are also associated with autoimmune inflammatory bowel diseases such as Coeliac and Crohn’s disease. Importantly, these unique T cells reside between nutrient-absorptive intestinal epithelial cells, close to the anaerobic microbes in the intestinal lumen. How IELs are able to respond to changes in intestinal epithelial cells and how they influence nutrition absorption and epithelial defence is currently unclear (1).
The aim of this project is to investigate how specific molecular regulators in IELs allows them to adapt to the intestinal microenvironment and mount appropriate responses to intestinal perturbations, including diet and microbial challenges. The discovery that PIM kinases uniquely regulate metabolic activation of IEL (2), and that T-cell receptor signalling in IEL is uniquely modified (3) , and that IEL have a unique metabolic signature (4), all suggest that changes in these molecular components are necessary for IELs to function. In this project, the student will learn to use state-of-the-art techniques including proteomics and phosphoproteomics, Ribo-Seq to rapidly identify changes in IEL, and in vivo models to address how perturbations in signalling pathways regulate intestinal homeostasis.
Deadline : 31 October 2025
(18) PhD Degree – Fully Funded
PhD position summary/title: TC1 – New technologies to monitor assembly of alternative forms of the proteasome
The PhD project aims to engineer the proteasome and develop new technologies to monitor the assembly of its alternative forms, in a format suitable for high-throughput screening. These tools will be instrumental in uncovering the functions of alternative proteasome complexes and in clarifying their involvement in disease. For example, mutations in proteasome subunits cause proteasomopathies (juvenile neurodevelopmental disorders), while mutations in proteasome-associated proteins are linked to early-onset Parkinson’s disease. Ultimately, this work will lay the foundation for novel strategies to restore protein homeostasis in neurodegenerative disorders. The project will offer training opportunities in state-of-the-art technologies such as cell engineering (CRISPR-Cas9 gene editing of proteasome genes), molecular biology (proteasome and protein degradation assays), and high-resolution confocal microscopy (proteasome dynamics).
Deadline :16 November 2025
(19) PhD Degree – Fully Funded
PhD position summary/title: TC2 – Cleave to Modify: A new biological mechanism for protein regulation
A striking example of this process comes from the ubiquitin-like domain (UBL) fusion proteins2. These proteins undergo proteolytic processing as a means of controlling their physiological roles3. We have recently discovered that the resulting fragments can be further modified with unprecedented post-translational modifications, a mechanism we refer to as “cleave-to-modify” (Figure1). This represents an entirely new layer of proteome regulation. However, very little is known about the UBL fusion protein family, the proteases responsible for their cleavage, or the downstream biological consequences of this mechanism.
This PhD project aims to identify novel substrates and pathways regulated by the “cleave-to-modify” mechanism and link these discoveries to cellular function. By doing so, the project will provide fundamental insights into how proteolytic processing diversifies protein function and reveal new opportunities for therapeutic intervention.
This project takes advantage of our recently developed toolkit to study UBL fusion proteins and their processing4. Students interested in gaining expertise in a wide variety of approaches are strongly encouraged to apply, since the project merges several disciplines, including: method development, state-of-the-art mass spectrometry, cell biology, biophysics, and biochemistry.
Deadline : 16 November 2025
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(20) PhD Degree – Fully Funded
PhD position summary/title: TC3 – Destroying cancer-causing proteins
This PhD project will explore precisely how FAM83D, FAM83F, and FAM83G regulate cell division and cancer cell proliferation, with a particular focus on their degradation as a therapeutic strategy. The project will employ a wide range of multi-disciplinary cutting-edge technologies, such as CRISPR/Cas9 genome editing, mass-spectrometry, DEL screens to identify ligands for FAM83D, FAM83F and FAM83G, and development and application of small molecule degraders, including PROTACs and molecular glues, against FAM83D-CK1-alpha, FAM83F-CK1-alpha and FAM83G-CK1-alpha complexes. The aim is to establish a mechanistic foundation and therapeutic rationale for selectively degrading these proteins complexes to suppress cancer cell growth.
Deadline : 16 November 2025
(21) PhD Degree – Fully Funded
PhD position summary/title: TC4 – How do Dysregulated Signalling Pathways cause Intellectual Disability?
This PhD project aims to map signalling pathways that are disrupted in intellectual disability, with the overarching goal of uncovering much-needed therapeutic opportunities in this area. The successful candidate will have the opportunity to utilise exciting new tools and reagents in the lab and expand on our recent progress in dissecting intellectual disability signalling networks. Potential approaches include (phospho)proteomic profiling mass-spectrometry, modelling human neural development using pluripotent stem cells, animal models of intellectual disability, cutting edge biochemistry, and structural analysis using Cryogenic Electron Microscopy (CryoEM). The student will be embedded in a dynamic team with a track record in dissecting intellectual disability signalling networks. They will also have excellent opportunities for further internal and external collaborations with leading experts in this area.
Deadline : 16 November 2025
(22) PhD Degree – Fully Funded
PhD position summary/title: TC5 – Finding the eat-me signals
The Ganley lab is interested in unravelling the molecular mechanism of autophagy (which literally translates from the Greek meaning to eat oneself). Autophagy is a critical lysosomal degradation pathway that functions to clear the cell of potentially damaging agents, such as protein aggregates or faulty mitochondria. Importantly, autophagy appears to be dysregulated in many diseases and therefore its modulation could lead to novel therapies. However, to enable this, we first need to understand the machinery involved.
A project is available to decipher the signals that lead to the specific autophagy of mitochondria (termed mitophagy), a process that has strong links to cancer and in particular Parkinson’s disease. Following up on recently published work, the project will utilise state-of-the-art microscopy, cell biology, protein biochemistry and mass spectrometry to identify phosphorylation and ubiquitylation events involved in capturing mitochondria for degradation. As well as gaining experience in a wide variety of techniques, you will be part of a dynamic and collaborative team intent on making new scientific discoveries and producing the next generation of world-class scientists.
Deadline : 16 November 2025
(23) PhD Degree – Fully Funded
PhD position summary/title: TC6 – Genome Bodyguards: Investigating the Cell’s Hidden Repair Team
The MMS22L–TONSL complex is a molecular “first responder” that helps cells protect and repair their DNA when it gets damaged during everyday life. In fact, when we use genome-editing to switch off this complex, cells die within one cell division. The problem is that without it, cells struggle to maintain the integrity of their genetic material—a problem at the heart of cancer, ageing, and many inherited diseases. Actually, TONSL overexpression has been linked to a range of cancers, and mutation in this gene cause debilitating symptoms. A major issue this that we don’t know how MMS22L-TONSL works at the molecular level. This state-of-the-art PhD project will explore how this complex works at the molecular level, discovering how it recognizes broken DNA, recruits repair machinery, and safeguards the stability of the genome. The project you’ll be part of is a collaboration with leading experts in genome maintenance around the world. By combining cutting-edge biochemistry, molecular biology, structural studies, and live-cell imaging, as well as genome-editing and genome-wide “-omic” technologies, the project aims to uncover new exciting insights into how cells defend themselves and how these processes can be harnessed in medicine.
Deadline : 16 November 2025
(24) PhD Degree – Fully Funded
PhD position summary/title: TC7 – Viral interference of ISG15 signals
One of the most important challenges facing biomedical research is to understand the molecular details of how our immune system defends against pathogens. In the Swatek lab, we aim to understand the roles of ubiquitin and ubiquitin-like modifications in the antiviral state (1). These modifications have emerged as crucial mediators of the signal transduction pathways that sense and respond to viruses. The ubiquitin-like protein, ISG15, is highly upregulated during viral infection and marks thousands of proteins to help shape the host defence response. To subvert ISG15 signalling, many viruses encode enzymes that remove these modifications, and we have previously identified an elegant example of viral-mediated ISG15 suppression (2). Surprisingly, however, the roles of the vast majority of ISG15 modifications are unknown, and therefore, understanding how ISG15 contributes to the antiviral state is of paramount importance. This PhD project aims to identify the ISG15 substrates targeted by viral effector proteins and link these discoveries to a cellular function.
This project takes advantage of our expansive toolkit to study the ISG15 system. Students interested in gaining expertise in a wide variety of approaches are strongly encouraged to apply since the project merges several disciplines, including method development, state-of-the-art mass spectrometry, cell biology, structural biology, biophysics, and biochemistry (3-4). The student will have the opportunity to participate in several internal and external collaborations.
Deadline : 16 November 2025
(25) PhD Degree – Fully Funded
PhD position summary/title: TC8 – Elucidating the physiological role of secretory pathway phosphorylations of key players of the complement pathway.
In the 1990s activated platelets were reported to release an unidentified inhibitor-resistant protein kinase outside the cell which phosphorylated multiple circulating plasma proteins including complement components and coagulation factors. In fact, preliminary data suggested that the phosphorylated complement components exhibited increased opsonization of immune complexes and higher binding efficiencies to the complement machinery. While secreted proteins have been known to be phosphorylated since the early 1880s, the identity of the kinase remained enigmatic for over 130 years. In 2012, a single kinase was shown to phosphorylate multiple substrates including the complement and coagulation factors. The preliminary data till date suggest that the kinase directly phosphorylates multiple complement components and coagulation factors stoichiometrically both in biochemical assays and in cells. Interestingly, platelets have rudimentary secretory pathway including Golgi which harbour the kinase. The key aims of the studentship are to:
- Understand how phosphorylation of coagulation and complement components alter their biochemical activities.
- Establish the effect of the secreted kinase on complement activity in human platelets and plasma
- Elucidate how platelet activation drives physiological roles of the secreted kinase using quantitative phosphoproteomics and activity assays from primary human and murine blood samples.
Deadline : 16 November 2025
(26) PhD Degree – Fully Funded
PhD position summary/title: TC9 – Investigating the effect of post translational modifications on Rare ApoE variants
In this proposal we plan to investigate the structural, receptor binding, and functional properties of these rare variants of ApoE using astrocyte, hepatocyte, and microglial derived ApoE. These different cell types differentially glycosylated APOE. We will also investigate the impact of these rare ApoE variants on neuroinflammation and amyloid aggregation and uptake using in house assays. We will then tie these results together to give greater understanding to the mechanisms by how this important element of the ApoE protein impacts the downstream processes. By studying these proteins in a wide battery of tests we hope to improve understanding of how each element of ApoE and the differences conferred by these single amino acid changes impacts the processes that increase or decrease AD risk.
Deadline : 16 November 2025
About The University of Dundee, Scotland, United Kingdom – Official Website
The University of Dundee[a] is a public research university based in Dundee, Scotland. It was founded as a university college in 1881 with a donation from the prominent Baxter family of textile manufacturers. The institution was, for most of its early existence, a constituent college of the University of St Andrews alongside United College and St Mary’s College located in the town of St Andrews itself. Following significant expansion, the University of Dundee gained independent university status by royal charter in 1967 while retaining elements of its ancient heritage and governance structure.
The main campus of the university is located in Dundee’s West End, which contains many of the university’s teaching and research facilities; the Duncan of Jordanstone College of Art and Design, Dundee Law School and the Dundee Dental Hospital and School. The university has additional facilities at Ninewells Hospital, containing its School of Medicine; Perth Royal Infirmary, which houses a clinical research centre; and in Kirkcaldy, Fife, containing part of its School of Health Sciences. The annual income of the institution for 2022–23 was £325.7 million of which £78.9 million was from research grants and contracts, with an expenditure of £330.2 million
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