Ron Hay’s Group (»Add to Infobox)

Link: Ron Hay Lab Group

General description: Role of ubiquitin and ubiquitin-like proteins in transcriptional regulation Ubiquitin and ubiquitin-like proteins are covalently linked to target proteins. While many polyubiquitinated proteins are destined to be degraded by the proteasome, modification by the ubiquitin-like proteins SUMO and NEDD8 are responsible for altering the function of target proteins. We have previously shown that the ubiquitin-like proteins have profound effects on gene expression and our objective is to define the function of these post-translational modifications in cellular metabolism. Using cell, molecular and structural biology we have defined the components required for modification and deconjugation and are in the process of determining their mechanism of action. Role in RUBICON: Although different SUMO family members show striking target specificity and differential regulation in vivo, currently known SUMO enzymes show virtually no preferences for different SUMO proteins in vitro. This suggests the existence of additional factors that recognize specific SUMO family members and contribute thereby to selectivity in vivo. These could be enzymes, enzyme co-factors or downstream effectors that protect specific target proteins from demodification. A comparative proteomic analysis will be performed to identify proteins that interact with a wild type SUMO substrate and mutants that can no longer be modified by SUMO.		Location of the promyelocytic leukaemia protein, PML (red) and the SUMO protease SENP2 (green) in a single nucleus. NMR analysis of the interaction between the SUMO E2 enzyme Ubc9 and the SUMO E3, RanBP2

MEMBERS (12/12)

Hay Ronald, Professor (Principal Investigator / Ron Hay’s Group)