The SH2-SH2-SH3 domain of phospholipase C-gamma 1 directly binds to translational elongation factor-1 alpha
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SCOPUS
- Title
- The SH2-SH2-SH3 domain of phospholipase C-gamma 1 directly binds to translational elongation factor-1 alpha
- Authors
- Kim, MJ; Si, F; Kim, SJ; Hong, SB; Hwang, JI; Lee, HJ; Lee, SJ; Chang, JS; Lee, YH; Ryu, SH; Suh, PG
- Date Issued
- 1999-12-31
- Publisher
- SPRINGER-VERLAG SINGAPORE PTE LTD
- Abstract
- Phospholipase C-gamma 1 (PLC-gamma 1) is a lipase that hydrolyzes PIP2 to generate two second messengers, IP3 and DAG, By using the yeast two-hybrid system, we identified the translational elongation factor-1 alpha (EF-1 alpha) as a binding protein of PLC-gamma 1 from the human B-lymphocyte library, Direct interaction between EF-1 alpha and PLC-gamma 1 was confirmed by the in vitro binding experiment using purified PLC-gamma 1, Furthermore, from the in vitro binding experiment, we could demonstrate that the carboxyl terminal region of EF-1 alpha is involved in the interaction with PLC-gamma 1, and that both SH2 and SH3 domains of PLC-gamma 1 are required for the interaction with EF-1 alpha. In vivo interaction between EF-1 alpha and PLC-gamma 1 was confirmed by the immunoprecipitation experiment using anti-EF-1 alpha antibody. The interaction between EF-1 alpha and PLC-gamma 1 was enhanced by EGF-treatment, Taken together, we suggest that EF-1 alpha might play a role in PLC-gamma 1-mediated signal transduction.
- Keywords
- EF-1 alpha; PLC-gamma 1; src homology domain; yeast two hybrid system; FACTOR EF-1-ALPHA; TYROSINE KINASE; FACTOR 1-ALPHA; C ISOZYMES; PROTEIN; CELLS; TRANSFORMATION; HOMOLOGY; DICTYOSTELIUM; SEQUENCE
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/20162
- ISSN
- 1016-8478
- Article Type
- Article
- Citation
- MOLECULES AND CELLS, vol. 9, no. 6, page. 631 - 637, 1999-12-31
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