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PMID: 8343130 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Non-catalytic activation of phospholipase C-gamma 1 in vitro by epidermal growth factor receptor.

The Biochemical journal ·Vol. 293 ( Pt 2) ·1993-07-15 ·Pages 507-11

Hernández-Sotomayor SM, Carpenter G

Abstract

To investigate the possible functional role of epidermal growth factor (EGF) receptor-phospholipase C-gamma 1 (PLC-gamma 1) complexes, we have measured PLC-gamma 1 activity in vitro in the absence or presence of purified EGF receptor. Immunoprecipitates of PLC-gamma 1 from control A-431 cells were incubated without or with purified EGF receptor in the absence or presence of ATP. Under these conditions the EGF receptor increased non-tyrosine-phosphorylated PLC-gamma 1 activity 3-4-fold in the absence or presence of ATP, but increased tyrosine-phosphorylated and activated PLC-gamma 1 by only 20-50%. Both basal and autophosphorylated forms of the purified EGF receptor increased the activity of the non-tyrosine-phosphorylated PLC-gamma 1, and stoichiometric levels of purified receptor were required to increase PLC activity. Other tyrosine kinases such as the platelet-derived growth factor receptor and erbB-2, but not the insulin receptor, also stimulated PLC-gamma 1 activity. PLC-gamma 1 activity could be activated with the kinase-negative EGF receptor, but a C-terminal truncated receptor was much less effective. Purified EGF receptor could also activate PLC-beta 1, but with a much decreased potency compared with PLC-gamma 1. Our results suggest that in vitro the EGF receptor can increase PLC-gamma 1 activity independently of tyrosine phosphorylation.

MeSH Terms
3T3 Cells Animals Catalysis Cattle Cells, Cultured Enzyme Activation ErbB Receptors/metabolism Isoenzymes/metabolism Mice Phosphorylation Substrate Specificity Type C Phospholipases/metabolism Tyrosine/metabolism
Chemicals
Isoenzymes Tyrosine ErbB Receptors Type C Phospholipases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hernández-Sotomayor S M
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146.
Carpenter G
References (32)
32 references, click to expand
  1. Altered distribution of phospholipase C-gamma 1 in benign hyperproliferative epidermal diseases.
    Cell Growth Differ. 1992 Apr;3(4):233-9 PMID: 1515369
  2. Receptor tyrosine kinase substrates: src homology domains and signal transduction.
    FASEB J. 1992 Nov;6(14):3283-9 PMID: 1385243
  3. Epidermal growth factor and a new derivative. Rapid isolation procedures and biological and chemical characterization.
    J Biol Chem. 1972 Dec 10;247(23):7609-11 PMID: 4636326
  4. Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor.
    J Biol Chem. 1979 Jun 10;254(11):4884-91 PMID: 312292
  5. A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles.
    J Biol Chem. 1982 Feb 10;257(3):1523-31 PMID: 6276390
  6. Characteristics of antibodies to the epidermal growth factor receptor-kinase.
    Arch Biochem Biophys. 1983 Dec;227(2):457-68 PMID: 6667027
  7. Specificity of the functional interactions of the beta-adrenergic receptor and rhodopsin with guanine nucleotide regulatory proteins reconstituted in phospholipid vesicles.
    J Biol Chem. 1985 Feb 10;260(3):1493-500 PMID: 2981858
  8. High-level expression of human insulin receptor cDNA in mouse NIH 3T3 cells.
    Proc Natl Acad Sci U S A. 1987 Aug;84(15):5237-41 PMID: 3299382
  9. Purification and characterization of two immunologically distinct phosphoinositide-specific phospholipases C from bovine brain.
    J Biol Chem. 1987 Sep 15;262(26):12511-8 PMID: 3040753
  10. Monoclonal antibodies to three phospholipase C isozymes from bovine brain.
    J Biol Chem. 1988 Oct 5;263(28):14497-504 PMID: 2459119
  11. Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium.
    Proc Natl Acad Sci U S A. 1989 Mar;86(5):1568-72 PMID: 2466293
  12. Studies of inositol phospholipid-specific phospholipase C.
    Science. 1989 May 5;244(4904):546-50 PMID: 2541501
  13. Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C.
    Proc Natl Acad Sci U S A. 1989 Nov;86(21):8232-6 PMID: 2554305
  14. Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.
    Mol Cell Biol. 1990 Feb;10(2):435-41 PMID: 2153914
  15. Specificity of receptor-G protein interactions. Discrimination of Gi subtypes by the D2 dopamine receptor in a reconstituted system.
    J Biol Chem. 1990 Mar 15;265(8):4507-14 PMID: 2137824
  16. The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C.
    Science. 1990 Mar 30;247(4950):1575-8 PMID: 2157283
  17. Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex.
    Mol Cell Biol. 1990 May;10(5):2359-66 PMID: 1691440
  18. Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors.
    Science. 1990 Nov 16;250(4983):979-82 PMID: 2173144
  19. Increase of the catalytic activity of phospholipase C-gamma 1 by tyrosine phosphorylation.
    Science. 1990 Nov 30;250(4985):1253-6 PMID: 1700866
  20. The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma.
    EMBO J. 1990 Dec;9(13):4375-80 PMID: 2176151
  21. Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation.
    Science. 1991 Mar 8;251(4998):1231-3 PMID: 1848725
  22. PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254.
    Cell. 1991 May 3;65(3):435-41 PMID: 1708307
  23. Multiple autophosphorylation site mutations of the epidermal growth factor receptor. Analysis of kinase activity and endocytosis.
    J Biol Chem. 1991 May 5;266(13):8355-62 PMID: 2022651
  24. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins.
    Science. 1991 May 3;252(5006):668-74 PMID: 1708916
  25. PLC gamma 1, a possible mediator of T cell receptor function.
    J Biol Chem. 1991 Sep 5;266(25):16277-80 PMID: 1832154
  26. A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1.
    Mol Cell Biol. 1991 Oct;11(10):5068-78 PMID: 1656221
  27. Elevated content of the tyrosine kinase substrate phospholipase C-gamma 1 in primary human breast carcinomas.
    Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10435-9 PMID: 1683701
  28. A site of tyrosine phosphorylation in the C terminus of the epidermal growth factor receptor is required to activate phospholipase C.
    Mol Cell Biol. 1992 Jan;12(1):128-35 PMID: 1729595
  29. SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma.
    EMBO J. 1992 Feb;11(2):559-67 PMID: 1537335
  30. Multiple autophosphorylation sites of the epidermal growth factor receptor are essential for receptor kinase activity and internalization. Contrasting significance of tyrosine 992 in the native and truncated receptors.
    J Biol Chem. 1992 Apr 25;267(12):8672-8 PMID: 1314835
  31. Growth factor stimulation of phospholipase C-gamma 1 activity. Comparative properties of control and activated enzymes.
    J Biol Chem. 1992 May 25;267(15):10447-56 PMID: 1316902
  32. Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma.
    EMBO J. 1992 Nov;11(11):3911-9 PMID: 1396585
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1993-07-15
Pages
507-11
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1134390
Subset
IM
Grants
NCI NIH HHS · CA43720 · United States
FIC NIH HHS · TW04600 · United States
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