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The SH2-SH2-SH3 domain of phospholipase C-gamma 1 directly binds to translational elongation factor-1 alpha

Title
The SH2-SH2-SH3 domain of phospholipase C-gamma 1 directly binds to translational elongation factor-1 alpha
Authors
Kim, MJSi, FKim, SJHong, SBHwang, JILee, HJLee, SJChang, JSLee, YHRyu, SHSuh, PG
POSTECH Authors
Ryu, SH
Date Issued
Jan-1999
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
http://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, 1999-01
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 RYU, SUNG HO
Dept of Life Sciences
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