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JCS ePress online publication date 25 May 2004
doi: 10.1242/jcs.01156

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Research Article

A NHERF binding site links the {beta}PDGFR to the cytoskeleton and regulates cell spreading and migration


Marianne F. James, Roberta L. Beauchamp, Nitasha Manchanda, Andrius Kazlauskas, and Vijaya Ramesh*
* Author for correspondence (e-mail: ramesh{at}helix.mgh.harvard.edu)

The Na+/H+ exchanger regulatory factor, NHERF, is a multifunctional adapter protein involved in a wide range of physiological activities. NHERF associates with merlin and the ezrin/radixin/moesin (MERM) family of membrane-actin cytoskeletal linker proteins through its C-terminus and is capable of interacting via its PDZ1 domain to the {beta}PDGF receptor ({beta}PDGFR). Thus, NHERF, potentially links the {beta}PDGFR to the actin cytoskeleton through its interaction with MERM proteins. In the present study, we have examined whether abolishing the interaction of {beta}PDGFR with NHERF results in actin cytoskeletal rearrangements. We have stably expressed a wild-type {beta}PDGFR, a mutant {beta}PDGFR (L1106A) that is incapable of interacting with NHERF, as well as a kinase defective mutant receptor (K634R), in PDGFR-deficient mouse embryonic fibroblasts. Our observations indicate that cells expressing {beta}PDGFR (L1106A) were impaired in their ability to spread and migrate on fibronectin compared with wild-type and K634R cells. L1106A mutant cells also revealed an increased number of focal adhesions, a condensed F-actin ring at the cell periphery and a decrease in total focal adhesion kinase (FAK) tyrosine phosphorylation. Further, we show that NHERF and MERM proteins could act as intermediary bridging proteins between {beta}PDGFR and FAK. Thus, the interaction of {beta}PDGFR with NHERF may provide an essential link between the cell membrane and the cortical actin cytoskeleton independent of receptor activity.
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