Rosine Haguenauer-Tsapis's Group (»Add to Infobox)

Rosine Haguenauer-Tsapis's Laboratory: Ubiquitin and Trafficking

General description: We are studying intracellular traffic along the endocytic and Golgi to vacuole trafficking pathways using budding yeast as a model organism. We largely contributed to the understanding that the main internalization signal in yeast is the modification of target plasma membrane proteins by covalent addition of ubiquitin, mediated by Rsp5p, the unique member in yeast of ubiquitin protein ligase of the Nedd4 family. . We demonstrated that two Rsp5 plasma membrane substrates undergo modification by UbK63-linked short chains. We are also studying the role played by Rsp5p in ubiquitylation leading to sorting to internal vesicles of the multivesicular body (MVB). Role in RUBICON: deciphering in a list of endocytic and MVB yeast substrates the occurrence of monoubiquitylation, and modification by UbK63 chains. In latter case, search for Rsp5 adapters potentially involved, Further characterization of the role of the C2 domain of the E3 Rsp5 and identification of potential partners identification of the potential role of ubiquitin isopeptidases involved at several steps of intracellular trafficking along the secretory, endocytic and recycling pathways analysis of ubiquitylation events involved in Golgi to vacuole sorting of plasma membrane transporters identification of E2/E3 pairs involved in ERAD of misfolded multispanning proteins like Fur4*		Multiple roles of Rsp5p in protein trafficking

MEMBERS (7/7)

Haguenauer-Tsapis Rosine (Principal Investigator / Rosine Haguenauer-Tsapis's Group)