JBC Papers in Press. Published on August 13, 2012, doi: 10.1074/jbc.M112.374652
GIT1 phosphorylation on serine 46 by PKD3 regulates paxillin trafficking and cellular protrusive activity
Bettina Huck 1, Ralf Kemkemer 2, Mirita Franz-Wachtel 3, Boris Macek 3, Angelika Hausser 1, and Monilola A. Olayioye 1,*
1University of Stuttgart, Institute of Cell Biology and Immunology, Allmandring 31, 70569 Stuttgart, Germany
2Department of New Materials and Biosystems, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, Stuttgart, Germany
3Proteome Center Tuebingen, Interfaculty Institute for Cell Biology, University of Tuebingen, Auf der Morgenstelle 15, 72076 Tuebingen, Germany
Correspondence: Professor Dr MA Olayioye, Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring 31, Baden-Württemberg, Stuttgart 70569, Germany. E-mail: firstname.lastname@example.org
Background: The multidomain protein GIT1 is involved in cytoskeletal
rearrangements and cell motility.
Results: GIT1 phosphorylation on serine 46 by PKD3 regulates localization of GIT1-paxillin complexes.
Conclusion: Paxillin trafficking and cellular protrusive activity are controlled by GIT1 serine 46 phosphorylation.
Significance: Selective phosphorylation of GIT1 by PKD3 implicates a specific function for this PKD isoform in the regulation of cell shape and motility.