Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 391, Issue 1, Pages 49-55Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.10.159
Keywords
pY27-caveolin-2; Insulin receptor; PTPs; SOCS-3; IRS-1; Rapamycin; pS727-STAT3
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Funding
- Ministry for Health. Welfare and Family affairs, Republic of Korea [0920110]
- Ministry of Education, Science and Technology, Korea
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Caveolin-2 regulation of insulin receptor (IR) tyrosine kinase activity was investigated. An insulin time course revealed that rapidly induced tylosine phosphorylation of IR was steadily maintained over a 180 min time period. In parallel, insulin-exerted IR interaction with caveolin-2 was detected as early as 5 min throughout until 180 min. Down-regulation of caveolin-2 by caveolin-2 siRNA arrested specifically a long term activation of IR. The attenuation of IR activation resulted in retardation of rapamycinsensitive pS727-STAT3 activation. As caveolin-2 tyrosine mutants were examined, Y27A-caveolin-2 explicitly impeded the long term IR activation by insulin, enhanced tyrosine dephosphorylation of IR, impaired tyrosine phosphorylation of IRS-1. and exerted the interaction between activated IR and SOCS-3 To.-ether. we propose that pY27-caveolin-2 prolongs IR activation by its interaction with IR, thereby preventing IR interaction with SOCS-3. (C) 2009 Elsevier Inc All rights reserved
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