Translocation of PLC-γ to the plasma membrane caused by truncated tyrosine kinases

Research output: Contribution to journalArticleResearchpeer-review

Abstract

PLC-γ activation correlates with PLC-γ tyrosine phosphorylation, association of PLC-γ with the EGF receptor and translocation of PLC-γ from the cytosol to the membrane. PLC-γ association with the EGF receptor and tyrosine phosphorylation of PLC-γ are required for activity. However, the importance and mechanism of PLC-γ translocation to the membrane for PIP 2 breakdown is unknown. PLC-γ translocation was studied in cell lines containing EGF receptor mutants that were unable to activate PLC-γ or associate with PLC-γ but were still capable of phosphorylating PLC-γ. Kinase active receptors which were unable to activate PLC-γ were still able to induce translocation of PLC-γ from the cytoplasm. Both wild type and autophosphorylation deficient receptors showed equivalent translocation with increasing EGF. Transport of PLC-γ from the cytosol was disrupted with triton X-100 suggesting that PLC-γ is associated with the membrane and not the cytoskeleton.

Original languageEnglish
Pages (from-to)393-398
Number of pages6
JournalJournal of Biochemistry, Molecular Biology and Biophysics
Volume5
Issue number5
StatePublished - 1 Dec 2001

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Cell membranes
Programmable logic controllers
Epidermal Growth Factor Receptor
Protein-Tyrosine Kinases
Cell Membrane
Cytosol
Membranes
Tyrosine
Phosphorylation
Octoxynol
Cytoskeleton
Epidermal Growth Factor
Cytoplasm
Phosphotransferases
Cell Line
Association reactions

Keywords

  • Membrane translocation
  • Phospholipase C
  • Tyrosine phosphorylation

Cite this

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abstract = "PLC-γ activation correlates with PLC-γ tyrosine phosphorylation, association of PLC-γ with the EGF receptor and translocation of PLC-γ from the cytosol to the membrane. PLC-γ association with the EGF receptor and tyrosine phosphorylation of PLC-γ are required for activity. However, the importance and mechanism of PLC-γ translocation to the membrane for PIP 2 breakdown is unknown. PLC-γ translocation was studied in cell lines containing EGF receptor mutants that were unable to activate PLC-γ or associate with PLC-γ but were still capable of phosphorylating PLC-γ. Kinase active receptors which were unable to activate PLC-γ were still able to induce translocation of PLC-γ from the cytoplasm. Both wild type and autophosphorylation deficient receptors showed equivalent translocation with increasing EGF. Transport of PLC-γ from the cytosol was disrupted with triton X-100 suggesting that PLC-γ is associated with the membrane and not the cytoskeleton.",
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Translocation of PLC-γ to the plasma membrane caused by truncated tyrosine kinases. / Vega, Quinn.

In: Journal of Biochemistry, Molecular Biology and Biophysics, Vol. 5, No. 5, 01.12.2001, p. 393-398.

Research output: Contribution to journalArticleResearchpeer-review

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