SOS1 as a regulator of phospholipase C-gl

Myung Jong Jkim, Jong Soo Chang, Fuchun Si, Jong-Ik Hwang, Sung H. Ryu, Pann Ghill Suhn

Research output: Contribution to journalArticle

Abstract

The SH3 domain of PLC-gl has been known to be responsible for the mitogenu effect of PLC-gl and also to be implicated in the control of the lipase activity of the PLC-gl protein. However, little is known about the putative effector pro teins that bind to the PLC-gl SH3 domain. We provide evidence that SOSl, one of the activators of p21 Ras, binds to the SH3 domain of PLC-gl. SOSl co-precipitated with the GST-fused SH3 domain of PLC-gl in vitro. The inter action between SOSl and PLC-gl is mediated by direct physical interaction. Moreover, the C-terminal proline-rich domain of SOSl is involved in the inter action with the PLC-gl SH3 domain. PLC-gl could be co-immunoprecipitated with SOSl antibody. The association between SOSl and SH3 domain of PLC-gl was not influenced by either the activation of the EGF receptor or v-Src-induced transformation in vitro. However, in vivo association between SOSl and PLCgl was slightly potenciated by the activation of EGF-receptor. Furthermore, in transient expression studies with COS-7 cells, we characterized the association between PLC-gl and SOSl in vivo. We could demonstrate that the SH3 domain of PLC-gl is absolutely required for the association with SOSl in vivo. SOSl over-expression in COS-7 cells inhibited EGF-induced Pi-turnover and EGFinduced tyrosyl phosphorylation of PLC-gl. Based on all these observations together, we propose that SOSl may act as a possible regulator in a PLC-gl mediated signaling pathway.

Original languageEnglish
JournalFASEB Journal
Volume12
Issue number8
Publication statusPublished - 1998 Dec 1
Externally publishedYes

Fingerprint

src Homology Domains
phospholipase C
Type C Phospholipases
Programmable logic controllers
proline
phosphorylation
cells
COS Cells
antibodies
Epidermal Growth Factor Receptor
Association reactions
Proto-Oncogene Proteins p21(ras)
proteins
epidermal growth factor receptors
Lipase
Epidermal Growth Factor
Proline
Chemical activation
Phosphorylation
Antibodies

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Jkim, M. J., Chang, J. S., Si, F., Hwang, J-I., Ryu, S. H., & Suhn, P. G. (1998). SOS1 as a regulator of phospholipase C-gl. FASEB Journal, 12(8).

SOS1 as a regulator of phospholipase C-gl. / Jkim, Myung Jong; Chang, Jong Soo; Si, Fuchun; Hwang, Jong-Ik; Ryu, Sung H.; Suhn, Pann Ghill.

In: FASEB Journal, Vol. 12, No. 8, 01.12.1998.

Research output: Contribution to journalArticle

Jkim, MJ, Chang, JS, Si, F, Hwang, J-I, Ryu, SH & Suhn, PG 1998, 'SOS1 as a regulator of phospholipase C-gl', FASEB Journal, vol. 12, no. 8.
Jkim MJ, Chang JS, Si F, Hwang J-I, Ryu SH, Suhn PG. SOS1 as a regulator of phospholipase C-gl. FASEB Journal. 1998 Dec 1;12(8).
Jkim, Myung Jong ; Chang, Jong Soo ; Si, Fuchun ; Hwang, Jong-Ik ; Ryu, Sung H. ; Suhn, Pann Ghill. / SOS1 as a regulator of phospholipase C-gl. In: FASEB Journal. 1998 ; Vol. 12, No. 8.
@article{b7ac21aa7bf949698170ba1baadc2c93,
title = "SOS1 as a regulator of phospholipase C-gl",
abstract = "The SH3 domain of PLC-gl has been known to be responsible for the mitogenu effect of PLC-gl and also to be implicated in the control of the lipase activity of the PLC-gl protein. However, little is known about the putative effector pro teins that bind to the PLC-gl SH3 domain. We provide evidence that SOSl, one of the activators of p21 Ras, binds to the SH3 domain of PLC-gl. SOSl co-precipitated with the GST-fused SH3 domain of PLC-gl in vitro. The inter action between SOSl and PLC-gl is mediated by direct physical interaction. Moreover, the C-terminal proline-rich domain of SOSl is involved in the inter action with the PLC-gl SH3 domain. PLC-gl could be co-immunoprecipitated with SOSl antibody. The association between SOSl and SH3 domain of PLC-gl was not influenced by either the activation of the EGF receptor or v-Src-induced transformation in vitro. However, in vivo association between SOSl and PLCgl was slightly potenciated by the activation of EGF-receptor. Furthermore, in transient expression studies with COS-7 cells, we characterized the association between PLC-gl and SOSl in vivo. We could demonstrate that the SH3 domain of PLC-gl is absolutely required for the association with SOSl in vivo. SOSl over-expression in COS-7 cells inhibited EGF-induced Pi-turnover and EGFinduced tyrosyl phosphorylation of PLC-gl. Based on all these observations together, we propose that SOSl may act as a possible regulator in a PLC-gl mediated signaling pathway.",
author = "Jkim, {Myung Jong} and Chang, {Jong Soo} and Fuchun Si and Jong-Ik Hwang and Ryu, {Sung H.} and Suhn, {Pann Ghill}",
year = "1998",
month = "12",
day = "1",
language = "English",
volume = "12",
journal = "The FASEB journal : official publication of the Federation of American Societies for Experimental Biology",
issn = "1530-6860",
publisher = "FASEB",
number = "8",

}

TY - JOUR

T1 - SOS1 as a regulator of phospholipase C-gl

AU - Jkim, Myung Jong

AU - Chang, Jong Soo

AU - Si, Fuchun

AU - Hwang, Jong-Ik

AU - Ryu, Sung H.

AU - Suhn, Pann Ghill

PY - 1998/12/1

Y1 - 1998/12/1

N2 - The SH3 domain of PLC-gl has been known to be responsible for the mitogenu effect of PLC-gl and also to be implicated in the control of the lipase activity of the PLC-gl protein. However, little is known about the putative effector pro teins that bind to the PLC-gl SH3 domain. We provide evidence that SOSl, one of the activators of p21 Ras, binds to the SH3 domain of PLC-gl. SOSl co-precipitated with the GST-fused SH3 domain of PLC-gl in vitro. The inter action between SOSl and PLC-gl is mediated by direct physical interaction. Moreover, the C-terminal proline-rich domain of SOSl is involved in the inter action with the PLC-gl SH3 domain. PLC-gl could be co-immunoprecipitated with SOSl antibody. The association between SOSl and SH3 domain of PLC-gl was not influenced by either the activation of the EGF receptor or v-Src-induced transformation in vitro. However, in vivo association between SOSl and PLCgl was slightly potenciated by the activation of EGF-receptor. Furthermore, in transient expression studies with COS-7 cells, we characterized the association between PLC-gl and SOSl in vivo. We could demonstrate that the SH3 domain of PLC-gl is absolutely required for the association with SOSl in vivo. SOSl over-expression in COS-7 cells inhibited EGF-induced Pi-turnover and EGFinduced tyrosyl phosphorylation of PLC-gl. Based on all these observations together, we propose that SOSl may act as a possible regulator in a PLC-gl mediated signaling pathway.

AB - The SH3 domain of PLC-gl has been known to be responsible for the mitogenu effect of PLC-gl and also to be implicated in the control of the lipase activity of the PLC-gl protein. However, little is known about the putative effector pro teins that bind to the PLC-gl SH3 domain. We provide evidence that SOSl, one of the activators of p21 Ras, binds to the SH3 domain of PLC-gl. SOSl co-precipitated with the GST-fused SH3 domain of PLC-gl in vitro. The inter action between SOSl and PLC-gl is mediated by direct physical interaction. Moreover, the C-terminal proline-rich domain of SOSl is involved in the inter action with the PLC-gl SH3 domain. PLC-gl could be co-immunoprecipitated with SOSl antibody. The association between SOSl and SH3 domain of PLC-gl was not influenced by either the activation of the EGF receptor or v-Src-induced transformation in vitro. However, in vivo association between SOSl and PLCgl was slightly potenciated by the activation of EGF-receptor. Furthermore, in transient expression studies with COS-7 cells, we characterized the association between PLC-gl and SOSl in vivo. We could demonstrate that the SH3 domain of PLC-gl is absolutely required for the association with SOSl in vivo. SOSl over-expression in COS-7 cells inhibited EGF-induced Pi-turnover and EGFinduced tyrosyl phosphorylation of PLC-gl. Based on all these observations together, we propose that SOSl may act as a possible regulator in a PLC-gl mediated signaling pathway.

UR - http://www.scopus.com/inward/record.url?scp=33749104541&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749104541&partnerID=8YFLogxK

M3 - Article

VL - 12

JO - The FASEB journal : official publication of the Federation of American Societies for Experimental Biology

JF - The FASEB journal : official publication of the Federation of American Societies for Experimental Biology

SN - 1530-6860

IS - 8

ER -