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JCS ePress online publication date 13 Jul 2004
doi: 10.1242/jcs.01220

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Research Article

Phospholipase C-{gamma}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*
* Author for correspondence (e-mail: pgs{at}postech.ac.kr)

Phospholipase C-{gamma}1 (PLC-{gamma}1), which interacts with a variety of signaling molecules through its two Src homology (SH) 2 domains and a single SH3 domain has been implicated in the regulation of many cellular functions. We demonstrate that PLC-{gamma}1 acts as a guanine nucleotide exchange factor (GEF) of dynamin-1, a 100 kDa GTPase protein, which is involved in clathrin-mediated endocytosis of epidermal growth factor (EGF) receptor. Overexpression of PLC-{gamma}1 increases endocytosis of the EGF receptor by increasing guanine nucleotide exchange activity of dynamin-1. The GEF activity of PLC-{gamma}1 is mediated by the direct interaction of its SH3 domain with dynamin-1. EGF-dependent activation of ERK and serum response element (SRE) are both up-regulated in PC12 cells stably overexpressing PLC-{gamma}1, but knockdown of PLC-{gamma}1 by siRNA significantly reduces ERK activation. These results establish a new role for PLC-{gamma}1 in the regulation of endocytosis and suggest that endocytosis of activated EGF receptors may mediate PLC-{gamma}1-dependent proliferation.
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