Merlin Phosphorylation by p21-activated Kinase 2 and Effects of Phosphorylation on Merlin Localization
pmid: 11782491
Merlin Phosphorylation by p21-activated Kinase 2 and Effects of Phosphorylation on Merlin Localization
The Nf2 tumor suppressor gene product merlin is related to the membrane-cytoskeleton linker proteins of the band 4.1 superfamily, including ezrin, radixin, and moesin (ERMs). Merlin is regulated by phosphorylation in a Rac/cdc42-dependent fashion. We report that the phosphorylation of merlin at serine 518 is induced by the p21-activated kinase PAK2. This is demonstrated by biochemical fractionation, use of active and dominant-negative mutants of PAK2, and immunodepletion. By using wild-type and mutated forms of merlin and phospho-directed antibodies, we show that phosphorylation of merlin at serine 518 leads to dramatic protein relocalization.
- University of New Hampshire United States
- Howard Hughes Medical Institute United States
- Massachusetts Institute of Technology United States
Neurofibromin 2, Time Factors, Swine, Blotting, Western, 3T3 Cells, Protein Serine-Threonine Kinases, Transfection, Cell Line, Protein Structure, Tertiary, Mice, p21-Activated Kinases, Mutation, Serine, Animals, Phosphorylation, cdc42 GTP-Binding Protein, Plasmids, Protein Binding, Signal Transduction, Subcellular Fractions
Neurofibromin 2, Time Factors, Swine, Blotting, Western, 3T3 Cells, Protein Serine-Threonine Kinases, Transfection, Cell Line, Protein Structure, Tertiary, Mice, p21-Activated Kinases, Mutation, Serine, Animals, Phosphorylation, cdc42 GTP-Binding Protein, Plasmids, Protein Binding, Signal Transduction, Subcellular Fractions
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