Translocation of PLC-Γ to the Plasma Membrane Caused By Truncated Tyrosine Kinases
Document Type
Article
Publication Date
12-1-2001
Journal / Book Title
Journal of Biochemistry, Molecular Biology and Biophysics
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.
Journal ISSN / Book ISBN
ISSN 1607-8527, 1025-8141
MSU Digital Commons Citation
Vega, Quinn, "Translocation of PLC-Γ to the Plasma Membrane Caused By Truncated Tyrosine Kinases" (2001). Department of Mathematics Facuty Scholarship and Creative Works. 184.
https://digitalcommons.montclair.edu/mathsci-facpubs/184
Published Citation
Vega, Q. (2001). Translocation of PLC-γ to the plasma membrane caused by truncated tyrosine kinases. Journal of Biochemistry, Molecular Biology and Biophysics, 5(5), 393-398.