Professor Jennifer Greaves

Supervisor Details

Contact Details

Centre for Health & Life Sciences, Coventry University

Scientific Background

Research Interests

Dr Greaves’ research uses a combination of cellular, molecular and chemical-biology techniques to investigate how the metabolic serine hydrolase enzymes regulate the posttranslational protein-lipid modification S-acylation (palmitoylation).

Supervision Style

In three words or phrases: supportive, collaborative, outcome-oriented.

Provision of Training

Your training will be supervised predominantly by myself and my experienced post docs/PhD students.

Progression Monitoring and Management

I like to be kept up to date, and will expect to see evidence of method development/data generation results on a weekly basis. I will expect you to take full ownership of your progression but will always be available to discuss a plan of action together. I am here for advice and guidance to help you reach the goals you set for yourself.

Communication

The team has a WhatsApp group chat with which we regularly communicate during the week. Whilst I expect you to keep up with team communications I will expect you to manage your work/life balance. I am happy to discuss any issues that are impacting your ability to fulfil your potential or my/our expectations. I am often available for ad hoc meetings outside our scheduled group and 1:1 meetings.

PhD Students can expect scheduled meetings with me:

In a group meeting

At least once a week

In year 1 of PhD study

At least once a week

In year 2 of PhD study

At least once a week

In year 3 of PhD study

At least once a week

These meetings will mainly be face to face, and I am usually contactable for an instant response on every working day.

Working Pattern

The timing of work in my lab is completely flexible, and (other than attending pre-arranged meetings), I expect students to manage their own time.

Notice Period for Feedback

I need at least 1 week’s notice to provide feedback on written work of up to 5000 words.

MIBTP Project Details

Primary supervisor for:

Molecular characterisation of the protein S-acylation machinery

See the PhD Opportunities section to see if this project is currently open for applications via MIBTP.

Please Note: The main page lists projects via BBSRC Research Theme(s) quoted and then relevant Topic(s).

Molecular characterisation of the protein S-acylation machinery

Secondary Supervisor(s): Dr Matthew Jenner

University of Registration: Coventry University

BBSRC Research Themes:

Understanding the Rules of Life (Immunology,Neuroscience and Behaviour,Structural Biology)
Integrated Understanding of Health (Ageing,Pharmaceuticals)

Project Outline

Protein S-acylation (commonly palmitoylation) is a reversible post-translational lipid modification in which fatty acids are attached to cysteine residues. This dynamic process is mediated by 'ZDHHC' family S-acyltransferases and protein deacylases (e.g., ABHD family enzymes), and it plays a critical role in regulating the localisation, stability, and activity of approximately 20% of the proteome. Dysregulation of S-acylation has been implicated in cancer, diabetes, and neurological disorders including schizophrenia, Huntington's disease, and Alzheimer's, highlighting the importance of understanding this modification [1]. However, despite its importance, the temporal and structural dynamics of protein S-acylation remain poorly defined. In particular, the interplay between S-acyltransferases, deacylases, and their substrates is not well understood at the molecular level [2].

This project aims to characterise the interactions between the S-acylation machinery and their substrate proteins using multidisciplinary approaches [3], including cell, molecular and chemical biology, protein biochemistry, confocal imaging and molecular modelling at Coventry University, as well as recently developed MS-based assays, namely carbene footprinting and native MS, at the University of Warwick. Together, these approaches will provide both a temporal and structural understanding of how dynamic S-acylation is regulated, how specificity is achieved, and how enzyme-substrate interactions contribute to the broader regulation of cellular function.

References:

1. F, S. M. et al. Nat Rev Mol Cell Biol 25, 488-509 (2024).

2. Abrami, L. et al. Nat Chem Biol 17, 438-447 (2021).

3. Greaves, J. et al. Proc Natl Acad Sci U S A 114, E1365-e1374 (2017).

Co-supervisor on projects with Dr Giuseppe Deganutti and Dr Matthew Jenner.