Identification and characterization of the interaction between heat-shock protein 90 and phospholipase C-gamma 1
SCIE
SCOPUS
- Title
- Identification and characterization of the interaction between heat-shock protein 90 and phospholipase C-gamma 1
- Authors
- Kim, SJ; Kim, MJ; Kim, Y; Si, FC; Ryu, SH; Suh, PG
- Date Issued
- 2000-03-31
- Publisher
- SPRINGER-VERLAG SINGAPORE PTE LTD
- Abstract
- Phosphoinositide-specific phospholipase C-gamma 1 (PLC-gamma 1) is a pivotal mediator in the signal transduction cascades induced by many growth factors. Using a yeast two-hybrid system, heat-shock protein 90 (Hsp90) was identified as a PLC-gamma 1-binding protein, A co-immunoprecipitation experiment, using anti-PLC-gamma 1 antibody, demonstrated an in vivo interaction between Hsp90 and PLC-gamma 1 in the NIH-3T3 cells. The interaction in NIH-3T3 was unaffected by the PDGF treatment, inducing phosphorylation and activation of PLC- gamma 1. Direct interaction between Hsp90 and PLC-gamma 1 was confirmed by in vitro binding experiments using purified Hsp90 and PLC-gamma 1. Furthermore, Hsp90 increased the PIP2-hydrolyzing activity of PLC-gamma 1 up to 2-fold at 0.1 mu M in vitro, Taken together, me show for the first time, the interaction of PLC-gamma 1 with Hsp90, both in vivo and in vitro. We suggest that Hsp90 may play a role in PLC-gamma 1-mediated signal transduction.
- Keywords
- Hsp90; in vitro binding experiment; PLC-gamma 1; protein-protein interaction; yeast two-hybrid system; EPIDERMAL-GROWTH-FACTOR; C ISOZYMES; ELEVATED CONTENT; DNA-SYNTHESIS; BOVINE BRAIN; CELLS; ACTIVATION; KINASE; PURIFICATION; RECEPTORS
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/20070
- ISSN
- 1225-8687
- Article Type
- Article
- Citation
- JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol. 33, no. 2, page. 97 - 102, 2000-03-31
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.