Phospholipase C-gamma 1 is a guanine nucleotide exchange factor for dynamin-1 and enhances dynamin-1-dependent epidermal growth factor receptor endocytosis
SCIE
SCOPUS
- Title
- Phospholipase C-gamma 1 is a guanine nucleotide exchange factor for dynamin-1 and enhances dynamin-1-dependent epidermal growth factor receptor endocytosis
- Authors
- Choi, JH; Park, JB; Bae, SS; Yun, S; Kim, HS; Hong, WP; Kim, IS; Kim, JH; Han, MY; Ryu, SH; Patterson, RL; Snyder, SH; Suh, PG
- Date Issued
- 2004-08-01
- Publisher
- COMPANY OF BIOLOGISTS LTD
- Abstract
- 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.
- Keywords
- phospholipase C-gamma 1; dynamin-1; guanine nucleotide exchange factor (GEF); endocytosis; proliferation; COATED VESICLE FORMATION; GTP-BINDING PROTEINS; DBL ONCOGENE PRODUCT; MEDIATED ENDOCYTOSIS; SIGNAL-TRANSDUCTION; MAP KINASE; POINT MUTATION; SH3 DOMAINS; RHO-GTPASES; C-GAMMA-1
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/17729
- DOI
- 10.1242/JCS.01220
- ISSN
- 0021-9533
- Article Type
- Article
- Citation
- JOURNAL OF CELL SCIENCE, vol. 117, no. 17, page. 3785 - 3795, 2004-08-01
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