Cell regulation by phosphotyrosine-targeted ubiquitin ligases.

Abstract:

:Three classes of E3 ubiquitin ligases, members of the Cbl, Hakai, and SOCS-Cul5-RING ligase families, stimulate the ubiquitination of phosphotyrosine-containing proteins, including receptor and nonreceptor tyrosine kinases and their phosphorylated substrates. Because ubiquitination frequently routes proteins for degradation by the lysosome or proteasome, these E3 ligases are able to potently inhibit tyrosine kinase signaling. Their loss or mutational inactivation can contribute to cancer, autoimmunity, or endocrine disorders, such as diabetes. However, these ligases also have biological functions that are independent of their ubiquitination activity. Here we review relevant literature and then focus on more-recent developments in understanding the structures, substrates, and pathways through which the phosphotyrosine-specific ubiquitin ligases regulate diverse aspects of cell biology.

journal_name

Mol Cell Biol

authors

Cooper JA,Kaneko T,Li SS

doi

10.1128/MCB.00098-15

subject

Has Abstract

pub_date

2015-06-01 00:00:00

pages

1886-97

issue

11

eissn

0270-7306

issn

1098-5549

pii

MCB.00098-15

journal_volume

35

pub_type

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