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Journal article

Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation.

Abstract:

Tyrosine kinase signaling is tightly controlled by negative feedback inhibitors including suppressors of cytokine signaling (SOCS). SOCS assemble as SH2 domain substrate recognition modules in ElonginB/C-cullin ubiquitin ligases. In accordance, SOCS4 reduces STAT3 signaling from EGFR through increased receptor degradation. Variable C-termini in SOCS4-SOCS7 exclude these family members from a SOCS2-type domain arrangement in which a strictly conserved C terminus determines domain packing. The ...

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Publication status:
Published

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Publisher copy:
10.1016/j.str.2007.09.016

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
Journal:
Structure (London, England : 1993) More from this journal
Volume:
15
Issue:
11
Pages:
1493-1504
Publication date:
2007-11-01
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
Language:
English
Keywords:
Pubs id:
pubs:34040
UUID:
uuid:a0ffbec3-f0f7-4840-b5a1-1279598d5e40
Local pid:
pubs:34040
Source identifiers:
34040
Deposit date:
2012-12-19

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