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Semin Cell Dev Biol. 2000 Jun;11(3):141-8.

Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome.

Author information

1
Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. genekdw@bimcore.emory.edu

Abstract

The post-translational modification of proteins by covalent attachment of ubiquitin targets these proteins for degradation by the proteasome. An astounding number of proteins are involved in ubiquitination and deubiquitination of proteins. The pathways are combinatorial, and selectivity of proteolysis will depend strongly on the exact combination of ubiquitinating and deubiquitinating enzymes present at any time. In addition to temporal control, it is likely that these modifications are also regulated spatially. In this review, we discuss the regulation of ubiquitination by enzymes of this pathway and highlight some of the outstanding problems in understanding this regulation.

PMID:
10906270
DOI:
10.1006/scdb.2000.0164
[Indexed for MEDLINE]

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