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Nat Cell Biol. 2004 Jun;6(6):523-31. Epub 2004 May 23.

Myosin-X provides a motor-based link between integrins and the cytoskeleton.

Author information

1
Karolinska Institutet, Department of Laboratory Medicine, Division of Pathology F46, Karolinska University Hospital Huddinge, SE-141 86 Huddinge, Sweden. hongquan.zhang@labmed.ki.se

Abstract

Unconventional myosins are actin-based motors with a growing number of attributed functions. Interestingly, it has been proposed that integrins are transported by unidentified myosins to facilitate cellular remodelling. Here we present an interaction between the unconventional myosin-X (Myo10) FERM (band 4.1/ezrin/radixin/moesin) domain and an NPXY motif within beta-integrin cytoplasmic domains. Importantly, knock-down of Myo10 by short interfering RNA impaired integrin function in cell adhesion, whereas overexpression of Myo10 stimulated the formation and elongation of filopodia in an integrin-dependent manner and relocalized integrins together with Myo10 to the tips of filopodia. This integrin relocalization and filopodia elongation did not occur with Myo10 mutants deficient in integrin binding or with a beta(1)-integrin point mutant deficient in Myo10 binding. Taken together, these results indicate that Myo10-mediated relocalization of integrins might serve to form adhesive structures and thereby promote filopodial extension.

PMID:
15156152
DOI:
10.1038/ncb1136
[Indexed for MEDLINE]

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