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Science. 2007 Jan 12;315(5809):201-5.

Proteasome-independent functions of ubiquitin in endocytosis and signaling.

Author information

1
Department of Biochemistry, University of Geneva, 30 Quai Ernest Ansermet, CH-1211 Geneva, Switzerland.

Abstract

Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76-amino acid polypeptide, ubiquitin, is primarily attached to the epsilon-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.

PMID:
17218518
DOI:
10.1126/science.1127085
[Indexed for MEDLINE]

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