Hyaluronan binding by CD44 is regulated by a phosphorylation-independent mechanism.

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Uff CR, Neame SJ, Isacke CM

Hyaluronan binding by CD44 is regulated by a phosphorylation-independent mechanism.

Eur J Immunol. 1995 Jul;25(7):1883-7. doi: 10.1002/eji.1830250714.

PubMed ID

7542594 [ View in PubMed

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Abstract

CD44 is an adhesion receptor for which the major characterized ligand is the extracellular matrix glycosaminoglycan, hyaluronan. This interaction underlies CD44-mediated cell attachment, cell migration, and matrix remodelling during development and wound healing. Truncation of the CD44 cytoplasmic domain does not prevent cell surface expression of this hyaluronan receptor but it dramatically impairs ligand binding. In this study we have examined the role of phosphorylation in regulating this function by mutating the target serine residues to either neutral amino acids with the aim of creating a phosphorylation-incompetent molecule, or to acidic residues to mimic a fully phosphorylated CD44. In transfected AKR1 cells the behavior of both the neutral and acidic mutants was indistinguishable from wild-type CD44, indicating that there is a phosphorylation-independent mechanism involved in regulating hyaluronan binding.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Hyaluronic acid	CD44 antigen	Protein	Humans	Yes	Binder	Details