Differential modification of Ras proteins by ubiquitination

Jura, N., Scotto-Lavino, E., Sobczyk, A., Bar-Sagi, D. (2006) Differential modification of Ras proteins by ubiquitination. Molecular Cell, 21 (5). pp. 679-687. ISSN 10972765

URL: http://www.ncbi.nlm.nih.gov/pubmed/16507365
DOI: 10.1016/j.molcel.2006.02.011

Abstract

Ras proteins are essential components of signal transduction pathways that control cell proliferation, differentiation, and survival. It is well recognized that the functional versatility of Ras proteins is accomplished through their differential compartmentalization, but the mechanisms that control their spatial segregation are not fully understood. Here we show that HRas is subject to ubiquitin conjugation, whereas KRas is refractory to this modification. The membrane-anchoring domain of HRas is necessary and sufficient to direct the mono- and diubiquitination of HRas. Ubiquitin attachment to HRas stabilizes its association with endosomes and modulates its ability to activate the Raf/MAPK signaling pathway. Therefore, differential ubiquitination of Ras proteins may control their location-specific signaling activities. ©2006 Elsevier Inc.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene regulation > transduction
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene regulation > transduction

bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > ubiquitin ligase
CSHL Authors:
Communities: CSHL labs > Svoboda lab
Depositing User: CSHL Librarian
Date: 2006
Date Deposited: 14 Dec 2011 16:03
Last Modified: 01 Mar 2013 15:17
Related URLs:
URI: http://repository.cshl.edu/id/eprint/22831

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