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 PIP2 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 language | English |
|---|---|
| Pages (from-to) | 393-398 |
| Number of pages | 6 |
| Journal | Journal of Biochemistry, Molecular Biology and Biophysics |
| Volume | 5 |
| Issue number | 5 |
| State | Published - 2001 |
Keywords
- Membrane translocation
- Phospholipase C
- Tyrosine phosphorylation