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Science 315 (5809): 201-205

Copyright © 2007 by the American Association for the Advancement of Science

Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling

Debdyuti Mukhopadhyay, and Howard Riezman*

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.

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

* To whom correspondence should be addressed. E-mail: Howard.Riezman{at}biochem.unige.ch

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Phosphoenolpyruvate Carboxylase from C4 Leaves Is Selectively Targeted for Inhibition by Anionic Phospholipids.
J. A. Monreal, F. McLoughlin, C. Echevarria, S. Garcia-Maurino, and C. Testerink (2010)
Plant Physiology 152, 634-638
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