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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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

Cited 15 times inthomson ciCited 18 times inthomson ci
Title
The SH2-SH2-SH3 domain of phospholipase C-gamma 1 directly binds to translational elongation factor-1 alpha
Author
Kim, Myung JongSi, FuchumKim, Su-JeongHong, Seung-BumHwang, Jong-IkLee, He-JinLee, Seung-JaeChang, Jong-SooLee, Young HanRyu, Sung HoSuh, Pann-Ghill
Issue Date
1999-12
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Citation
MOLECULES AND CELLS, v.9, no.6, pp.631 - 637
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
URI
https://scholarworks.unist.ac.kr/handle/201301/16454
URL
http://www.molcells.org/journal/view.html?year=1999&volume=9&number=6&spage=631
ISSN
1016-8478
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