Nature Cell Biology6, 523 - 531 (2004)
Published online: 23 May 2004; | doi:10.1038/ncb1136
Myosin-X provides a motor-based link between integrins and the cytoskeleton
Hongquan Zhang1, 2, Jonathan S. Berg3, Zhilun Li1, Yunling Wang1, Pernilla Lång1, Aurea D. Sousa3, Aparna Bhaskar3, Richard E. Cheney3
& Staffan Strömblad1
1
Karolinska Institutet, Department of Laboratory Medicine, Division of Pathology F46, Karolinska University Hospital Huddinge, SE-141 86 Huddinge, Sweden.
2
Department of Gastroenterology and Institute of Gastroenterology, Nanfang Hospital, the First Military Medical University, Guangzhou 510515, P.R. China.
3
Department of Cell and Molecular Physiology, University of North Carolina at Chapel Hill, NC 27599, USA.
Unconventional myosins are actin-based motors with a growing number of attributed functions1. Interestingly, it has been proposed that integrins are transported by unidentified myosins to facilitate cellular remodelling2. Here we present an interaction between the unconventional myosin-X (Myo10) FERM (band 4.1/ezrin/radixin/moesin) domain and an NPXY motif within -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 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.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
-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 
