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 -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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7, 65-70
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Ubiquitin carboxyl-terminal hydrolase L1 is required for maintaining the structure and function of the neuromuscular junction.

F. Chen, Y. Sugiura, K. G. Myers, Y. Liu, and W. Lin (2010)
PNAS 107, 1636-1641
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The ubiquitin-proteasome system in cardiac proteinopathy: a quality control perspective.

H. Su and X. Wang (2010)
Cardiovasc Res 85, 253-262
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Regulation of the endothelial cell cycle by the ubiquitin-proteasome system.

P. Fasanaro, M. C. Capogrossi, and F. Martelli (2010)
Cardiovasc Res 85, 272-280
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Stressing the ubiquitin-proteasome system.

N. P. Dantuma and K. Lindsten (2010)
Cardiovasc Res 85, 263-271
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The Deubiquitinating Enzyme BAP1 Regulates Cell Growth via Interaction with HCF-1.

Y. J. Machida, Y. Machida, A. A. Vashisht, J. A. Wohlschlegel, and A. Dutta (2009)
J. Biol. Chem. 284, 34179-34188
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