UNIGE document Scientific Article
previous document  unige:13118  next document
add to browser collection

Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling

Published in Science. 2007, vol. 315, no. 5809, p. 201 - 205
Abstract Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76–amino acid polypeptide, ubiquitin, is primarily attached to the e-amino group of lysines in target proteins. Ubiquitination is a major player in regulating a broad host of cellular processes, including cell division, differentiation, signal transduction, protein trafficking, and quality control. Aberrations in the ubiquitination system are implicated in pathogenesis of some diseases, certain malignancies, neurodegenerative disorders, and pathologies of the inflammatory immune response. Here, we discuss the proteasome-independent roles of ubiquitination in signaling and endocytosis.
Full text
(ISO format)
MUKHOPADHYAY, Debdyuti, RIEZMAN, Howard. Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling. In: Science, 2007, vol. 315, n° 5809, p. 201 - 205. https://archive-ouverte.unige.ch/unige:13118

174 hits

0 download


Deposited on : 2011-01-06

Export document
Format :
Citation style :