Postgraduate research opportunities Defining the Substrate Networks of ZDHHC Enzymes
ApplyKey facts
- Opens: Friday 25 March 2022
- Number of places: 1
- Duration: 3-4 years
Overview
S-acylation is an essential post-translational modification that regulates the localisation, stability, and function of a diverse array of proteins, including receptors, ion channels, transporters, signalling molecules, and chaperones. Defects in S-acylation are associated with cancer and neurological disorders.Eligibility
Equivalent to 2(i) Honours degree or Masters qualification.
Project Details
S-Acylation is a reversible post-translational modification that has been detected on over 4,000 mammalian proteins. This modification occurs on both soluble and transmembrane (TM) proteins and is catalysed by a large family of “zDHHC” enzymes that are present on membranes throughout the cell but strongly enriched in the early secretory pathway (endoplasmic reticulum (ER) and Golgi). Despite the importance of this modification in regulating protein stability and localisation, how S-acylation reactions are coordinated and the substrate networks of individual zDHHC enzymes are poorly defined areas.
The aims of this project are to:
- Identify the substrate networks of specific zDHHC enzymes.
- Identify conserved features of substrates that mediate recognition by zDHHC enzymes.
- Determine the importance of S-acylation of these substrates for cellular function.
Apply
Please apply via the PhD Pharmacy & Biomedical Sciences course page.
Number of places: 1
To read how we process personal data, applicants can review our 'Privacy Notice for Student Applicants and Potential Applicants' on our Privacy notices' web page.