Inositol 5′-phosphatase, SHIP1 interacts with phospholipase C-γ1 and modulates EGF-induced PLC activity

Minseok Song; Myung Jong Kim; Sanghoon Ha; Jong Bae Park; Sung Ho Ryu; Pann Ghill Sun

doi:10.1038/emm.2005.22

Inositol 5′-phosphatase, SHIP1 interacts with phospholipase C-γ1 and modulates EGF-induced PLC activity

Minseok Song, Myung Jong Kim, Sanghoon Ha, Jong Bae Park, Sung Ho Ryu, Pann Ghill Sun^*

^*Corresponding author for this work

Neurology

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

Phospholipase C-γ1, 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-γ1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIP1 as the binding protein for the SH3 domain of PLC-γ1. SHIP1 was co-immunoprecipitated with PLC-γ1 and potentiated EGF-induced PLC-γ1 activation. However, inositol 5′-phosphatase activity of SHIP1 was not required for the potentiation of EGF-induced PLC-γ1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-γ1 activation without regards to its inositol 5′-phosphatase activity.

Original language	English (US)
Pages (from-to)	161-168
Number of pages	8
Journal	Experimental and Molecular Medicine
Volume	37
Issue number	3
DOIs	https://doi.org/10.1038/emm.2005.22
State	Published - Jun 30 2005

Keywords

Epidermal growth factor
Phospholipase C-γ1
SH2 domain-containing inositol 5γ-phosphatase
SH3 domain

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Clinical Biochemistry

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title = "Inositol 5′-phosphatase, SHIP1 interacts with phospholipase C-γ1 and modulates EGF-induced PLC activity",

abstract = "Phospholipase C-γ1, 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-γ1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIP1 as the binding protein for the SH3 domain of PLC-γ1. SHIP1 was co-immunoprecipitated with PLC-γ1 and potentiated EGF-induced PLC-γ1 activation. However, inositol 5′-phosphatase activity of SHIP1 was not required for the potentiation of EGF-induced PLC-γ1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-γ1 activation without regards to its inositol 5′-phosphatase activity.",

keywords = "Epidermal growth factor, Phospholipase C-γ1, SH2 domain-containing inositol 5γ-phosphatase, SH3 domain",

author = "Minseok Song and Kim, {Myung Jong} and Sanghoon Ha and Park, {Jong Bae} and Ryu, {Sung Ho} and Sun, {Pann Ghill}",

year = "2005",

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doi = "10.1038/emm.2005.22",

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volume = "37",

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AU - Song, Minseok

AU - Kim, Myung Jong

AU - Ha, Sanghoon

AU - Park, Jong Bae

AU - Ryu, Sung Ho

AU - Sun, Pann Ghill

PY - 2005/6/30

Y1 - 2005/6/30

N2 - Phospholipase C-γ1, 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-γ1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIP1 as the binding protein for the SH3 domain of PLC-γ1. SHIP1 was co-immunoprecipitated with PLC-γ1 and potentiated EGF-induced PLC-γ1 activation. However, inositol 5′-phosphatase activity of SHIP1 was not required for the potentiation of EGF-induced PLC-γ1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-γ1 activation without regards to its inositol 5′-phosphatase activity.

AB - Phospholipase C-γ1, 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-γ1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIP1 as the binding protein for the SH3 domain of PLC-γ1. SHIP1 was co-immunoprecipitated with PLC-γ1 and potentiated EGF-induced PLC-γ1 activation. However, inositol 5′-phosphatase activity of SHIP1 was not required for the potentiation of EGF-induced PLC-γ1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-γ1 activation without regards to its inositol 5′-phosphatase activity.

KW - Epidermal growth factor

KW - Phospholipase C-γ1

KW - SH2 domain-containing inositol 5γ-phosphatase

KW - SH3 domain

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Inositol 5′-phosphatase, SHIP1 interacts with phospholipase C-γ1 and modulates EGF-induced PLC activity

Abstract

Keywords

ASJC Scopus subject areas

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