التفاصيل البيبلوغرافية
| العنوان: |
Cbl Competitively Inhibits Epidermal Growth Factor-induced Activation of Phospholipase C-...1. |
| المؤلفون: |
Jang Hyun Choi, Sun Sik Bae, Jong Bae Park, Sang Hoon Ha, Hebok Song, Jae-Ho Kim, Lucio Cocco, Sung Ho Ryu, Pann-Ghill Suh |
| المصدر: |
Molecules & Cells (Springer Science & Business Media B.V.); 2003, Vol. 15 Issue 2, p245, 11p |
| مصطلحات موضوعية: |
PHOSPHOLIPASES, CELL growth, CELL proliferation, GROWTH factors, SOMATOTROPIN, CARRIER proteins |
| مستخلص: |
Phospholipase C-γ1 (PLC-γ1) plays pivotal roles in cellular growth and proliferation through its two Src homology (SH) 2 domains and its single SH3 domain, which interact with signaling molecules in response to various growth factors and hormones. However, the role of the SH domains in the growth factor-induced regulation of PLC-γ1 is unclear. By peptide-mass fingerprinting analysis we have identified Cbl as a binding protein for the SH3 domain of PLC-γ1 from rat pheochromatocyte PC 12 cells. Association of Cbl with PLC-γ1 was induced by epidermal growth factor (EGF) but not by nerve growth factor (NGF). Upon EGF stimulation, both Cbl and PLC-γ1 were recruited to the activated EGF receptor through their SH2 domains. Mutation of the SH2 domains of either Cbl or PLC-γ1 abrogated tire EGF-induced interaction of PLC-γ1 with Cbl, indicating that SH2-mediated translocation is essential for the association of PLC-γ1 and Cbl. Overexpression of Cbl attenuated EGF-induced tyrosine phosphorylation and the subsequent activation of PLC-γ1 by interfering competitively with the interaction between PLC-γ1 and EGFR. Taken together, these results provide the first indications that Cbl may be a negative regulator of intracellular signaling following EGF-induced PLC-γ1 activation. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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