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The SOCS box—Adapting proteins for ubiquitination and proteasomal degradation
Author(s) -
Linossi Edmond M.,
Nicholson Sandra E.
Publication year - 2012
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1011
Subject(s) - f box protein , ubiquitin ligase , ubiquitin , signal transducing adaptor protein , ankyrin repeat , microbiology and biotechnology , proteasome , scaffold protein , sh2 domain , suppressor of cytokine signalling , biology , ubiquitin protein ligases , biochemistry , signal transduction , socs3 , gene , stat3 , proto oncogene tyrosine protein kinase src
The s uppressor o f c ytokine s ignalling (SOCS) box was first identified in the SH2‐containing SOCS box family (cytokine‐inducible SH2‐containing protein, SOCS1–7) and is a 40‐amino acid motif, which functions to recruit an E3 ubiquitin ligase complex consisting of the adapter proteins elongins B and C, Rbx2 and the scaffold protein Cullin5. The SOCS box is found in a diverse array of intracellular signalling molecules, many of which contain different protein interaction domains such as SPRY and WD40 domains, leucine and ankyrin repeats or other functional domains such as GTPases. In general, the SOCS box‐containing proteins are thought to act as substrate‐recognition modules to mediate the polyubiquitination and subsequent degradation of substrate proteins by the 26S proteasome. © 2012 IUBMB Life, 64(4): 316–323, 2012