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

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Inositol 5 '-phosphatase, SHIP1 interacts with phospholipase C-gamma 1 and modulates EGF-induced PLC activity

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Title
Inositol 5 '-phosphatase, SHIP1 interacts with phospholipase C-gamma 1 and modulates EGF-induced PLC activity
Author
Song, MKim, MJHa, SPark, JBRyu, SHSuh, PG
Issue Date
2005-06
Publisher
KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
Citation
EXPERIMENTAL AND MOLECULAR MEDICINE, v.37, no.3, pp.161 - 168
Abstract
Phospholipase C-gamma 1, containing two SH2 and one SH3 domains which participate in the interaction between signaling molecules, plays a significant role in the growth factor-induced signal transduction. However, the role of the SH domains in the growth factor-induced PLC-gamma 1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIN as the binding protein for the SH3 domain of PLC-gamma 1. SHIP1 was co-immunoprecipitated with PLC-gamma 1 and potentiated EGF-induced PLC-gamma 1 activation. However, inositol 5'-phosphatase activity of SHIN was not required for the potentiation of EGF-induced PLC-gamma 1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-gamma 1 activation without regards to its inositol 5'-phosphatase activity.
URI
https://scholarworks.unist.ac.kr/handle/201301/10828
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=22244447751
ISSN
1226-3613
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BIO_Journal Papers
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