What is it about?
We identified alpha-tubulin as a target of protein kinase Calpha. Specifically PKC phosphorylates Ser165. Mutation at Ser165 to an Asp residue (phosphomimetic) reproduces the motility phenotype that we ascribed to PKC activity, whereas mutation to Asn (blocks phosphorylation), slowed motility of intrinsically motile human breast tumor cells.
Featured Image
Why is it important?
Identifies an important target of this enzyme PKC which is instrumental in driving metastatic potential.
Perspectives
Please see the subsequent publications in which we delve more deeply into the significance of this site of phosphorylation in alpha-tubulin.
Dr Susan A. Rotenberg
Queens College- CUNY
Read the Original
This page is a summary of: Phosphorylation of α6-Tubulin by Protein Kinase Cα Activates Motility of Human Breast Cells, Journal of Biological Chemistry, April 2009, American Society for Biochemistry & Molecular Biology (ASBMB),
DOI: 10.1074/jbc.m902005200.
You can read the full text:
Contributors
The following have contributed to this page
