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Publication : The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha.

First Author  Miyake S Year  1998
Journal  Proc Natl Acad Sci U S A Volume  95
Issue  14 Pages  7927-32
PubMed ID  9653117 Mgi Jnum  J:48737
Mgi Id  MGI:1274932 Doi  10.1073/pnas.95.14.7927
Citation  Miyake S, et al. (1998) The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha. Proc Natl Acad Sci U S A 95(14):7927-32
abstractText  The Cbl protooncogene product has emerged as a negative regulator of receptor and non-receptor tyrosine kinases. We recently demonstrated that oncogenic Cbl mutants upregulate the endogenous tyrosine kinase signaling machinery when expressed in the NIH 3T3 cells, and identified the platelet-derived growth factor receptor-alpha (PDGFRalpha) as one of the tyrosine kinases targeted by these oncogenes. These findings suggested a role for the normal Cbl protein in negative regulation of the PDGFRalpha. However, the mechanism of such negative regulation remained to be determined. Here we show that overexpression of the wild-ubiquitination and degradation of receptor tyrosine kinases and suggest one potential mechanism for evolutionarily conserved negative regulatory influence of Cbl on tyrosine kinases.
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