You are here : Home > Scientific production > Discovery of ubiquitination as a new regulatory mechanism for ESCRT-III CHMP1B protein

Xènia Crespo-Yanez

Discovery of ubiquitination as a new regulatory mechanism for ESCRT-III CHMP1B protein

Published on 13 October 2017


Thesis presented on October 13, 2017

Abstract:
My thesis concerns the biogenesis of vesicles within an intracellular compartment specialized in the recycling or destruction of membrane receptors. This sorting of the receptors following their internalization by endocytosis from the surface towards the inside of the cell directly regulates the response to extracellular signals during development and adult life. The results presented demonstrate the existence and role of binding of a ubiquitin molecule in the activation of the endocytic protein (CHMP1B) in response to cell growth and differentiation factor (EGF) or to inflammatory cytokines (TNFa, IL1). In addition, they show the role of a protease (UBPY syn. USP8) in the hydrolysis of this ubiquitin and the polymerization of CHMP1B at the membrane. This new concept allows to better understand the mechanisms of deformation and scission of intracellular membranes in physiological or pathological processes.


Keywords:
Endocytosis, EGF receptor (EGFR), ESCRT-III, Intracellular trafficking, Multivesicular bodies (MVB), Oligomers, Ubiquitin, UBPY, USP8, deubiquitinase (DUB)

Download this thesis.