A Caltech Library Service

The Ubiquitin System and the N-End Rule Pathway

Varshavsky, Alexander and Turner, Glenn and Du, Fangyong and Xie, Youming (2000) The Ubiquitin System and the N-End Rule Pathway. Biological Chemistry, 381 (9-10). pp. 779-789. ISSN 1431-6730. doi:10.1515/BC.2000.101.

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item:


Eukaryotes contain a highly conserved multienzyme system which covalently links a small protein, ubiquitin, to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, an ATP-dependent protease. Pathways that involve ubiquitin play major roles in a huge variety of processes, including cell differentiation, cell cycle, and responses to stress. In this article we briefly review the design of the ubiquitin system, and describe two recent advances, the finding that ubiquitin ligases interact with specific components of the 26S proteasome, and the demonstration that peptides accelerate their uptake into cells by activating the N-end rule pathway, one of several proteolytic pathways of the ubiquitin system.

Item Type:Article
Related URLs:
URLURL TypeDescription
Varshavsky, Alexander0000-0002-4011-258X
Additional Information:© 2000 by Walter de Gruyter GmbH.
Issue or Number:9-10
Record Number:CaltechAUTHORS:20180803-074725065
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:88554
Deposited By: Tony Diaz
Deposited On:03 Aug 2018 15:02
Last Modified:16 Nov 2021 00:27

Repository Staff Only: item control page