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First published online July 30, 2004

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Not just a phospholipase

Phospholipase C-1 (PLC-1) is a critical signalling molecule in the regulation of cell proliferation. Its downstream effects depend both on its lipase activity – through which it generates inositol 1,4,5-trisphosphate and diacylglycerol – and on its SH2 and SH3 domains. Now, Pann-Ghill Suh and co-workers report that PLC-1 is also a guanine nucleotide exchange factor (GEF) that regulates the GTPase dynamin 1 and suggest that it is involved in the regulation of endocytosis (see p. 3785). Dynamin 1 drives clathrin-mediated endocytosis of numerous proteins, including growth factor receptors. In their paper, the authors show that PLC-1 functions as a dynamin 1 GEF in vitro and in vivo through a direct interaction between its SH3 domain and the GTPase. Overexpression of PLC-1 in PC12 cells enhances dynamin-1-dependent endocytosis of epidermal growth factor (EGF) receptor and as a result stimulates activation of the MAP kinase ERK, which is downstream of the EGF receptor. By contrast, downregulation of PLC-1 by siRNA reduces ERK activation. Suh and co-workers propose that PLC-1 functions as a key molecule in growth-factor-induced proliferation by regulating growth factor endocytosis.

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Phospholipase C-1 is a guanine nucleotide exchange factor for dynamin-1 and enhances dynamin-1-dependent epidermal growth factor receptor endocytosis

Jang Hyun Choi, Jong Bae Park, Sun Sik Bae, Sanguk Yun, Hyeon Soo Kim, Won-Pyo Hong, Il-Shin Kim, Jae Ho Kim, Mi Young Han, Sung Ho Ryu, Randen L. Patterson, Solomon H. Snyder, and Pann-Ghill Suh
JCS 2004 117: 3785-3795. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content