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Ca(2+)/calmodulin-dependent protein kinase mediates the phosphorylation of CD44 required for cell migration on hyaluronan

Lewis, Charlotte A., Townsend, Paul A. and Isacke, Clare M. (2001) Ca(2+)/calmodulin-dependent protein kinase mediates the phosphorylation of CD44 required for cell migration on hyaluronan Biochemical Journal, 357, (3), pp. 843-850.

Record type: Article


CD44 is the principal cell surface receptor for the extracellular matrix glycosaminoglycan hyaluronan, and binding to this ligand underlies CD44-mediated cell attachment and migration. As would be expected for a widely expressed adhesion receptor, CD44 is subject to complex regulatory events, and mis-regulation of the receptor has been associated with a number of disease pathologies, including chronic inflammatory conditions and the progression of metastatic tumours. In previous studies we have demonstrated that a key control point for this receptor is the phosphorylation of CD44 on a conserved cytoplasmic serine residue, Ser325. This modification is not required for efficient ligand binding, but is an essential component of CD44-dependent cell migration on a hyaluronan substratum. To understand better the mechanism regulating CD44 phosphorylation on Ser325, we have generated a monoclonal antibody that specifically recognizes CD44 phosphorylated on Ser325, and have developed assays to identify the Ser325 kinase. We demonstrate here that CD44 is phosphorylated to high stoichiometry in resting cells and that Ca2+/calmodulin-dependent protein kinase II is a CD44 Ser325 kinase.

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Published date: 2001
Keywords: adhesion, extracellular matrix, glycosaminoglycan, receptor


Local EPrints ID: 24833
ISSN: 1470-8728
PURE UUID: 2704e7a0-9c95-4e7d-8c8a-1be123d216e6

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Date deposited: 05 Apr 2006
Last modified: 17 Jul 2017 16:12

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