Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling
Top Cited Papers
- 12 January 2007
- journal article
- review article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 315 (5809), 201-205
- https://doi.org/10.1126/science.1127085
Abstract
Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76–amino acid polypeptide, ubiquitin, is primarily attached to the ϵ-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.Keywords
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