Phospholipase C-γ1 is a guanine nucleotide exchange factor for dynamin-1 and enhances dynamin-1-dependent epidermal growth factor receptor endocytosis | Zendy

Jang Hyun Choi | Zendy; Jong Bae Park | Zendy; Sun Sik Bae | Zendy; Sanguk Yun | Zendy; Hyeon Soo Kim | Zendy; Won-Pyo Hong | Zendy; Il-Shin Kim | Zendy; Jae Ho Kim | Zendy; Mi Young Han | Zendy; Sung Ho Ryu | Zendy; Randen L. Patterson | Zendy; Solomon H. Snyder | Zendy; PannGhill Suh | Zendy

Open Access

Phospholipase C-γ1 is a guanine nucleotide exchange factor for dynamin-1 and enhances dynamin-1-dependent epidermal growth factor receptor endocytosis

Author(s) -

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,

PannGhill Suh

Publication year - 2004

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.01220

Subject(s) - dynamin , guanine nucleotide exchange factor , endocytosis , biology , microbiology and biotechnology , epidermal growth factor , gtpase , proto oncogene tyrosine protein kinase src , sh3 domain , phospholipase c , phospholipase d , epidermal growth factor receptor , signal transduction , receptor , biochemistry

Phospholipase C-gamma1 (PLC-gamma1), 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-gamma1 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-gamma1 increases endocytosis of the EGF receptor by increasing guanine nucleotide exchange activity of dynamin-1. The GEF activity of PLC-gamma1 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-gamma1, but knockdown of PLC-gamma1 by siRNA significantly reduces ERK activation. These results establish a new role for PLC-gamma1 in the regulation of endocytosis and suggest that endocytosis of activated EGF receptors may mediate PLC-gamma1-dependent proliferation.

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