Myosin-X: a MyTH-FERM myosin at the tips of filopodia

被引:111
作者
Kerber, Michael L. [1 ]
Cheney, Richard E. [1 ]
机构
[1] Univ N Carolina, Sch Med, Dept Cell & Mol Physiol, Chapel Hill, NC 27599 USA
关键词
Myosin-X; Myo10; Filopodia; MyTH4-FERM; Intrafilopodial motility; CALMODULIN-LIKE PROTEIN; UNCONVENTIONAL MYOSIN; ACTIN-FILAMENTS; MOLECULAR MOTOR; CARGO RECOGNITION; BUNDLED ACTIN; DOMAIN; CELLS; BINDING; DYNAMICS;
D O I
10.1242/jcs.023549
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Myosin-X (Myo10) is an unconventional myosin with MyTH4-FERM domains that is best known for its striking localization to the tips of filopodia and its ability to induce filopodia. Although the head domain of Myo10 enables it to function as an actin-based motor, its tail contains binding sites for several molecules with central roles in cell biology, including phosphatidylinositol (3,4,5)-trisphosphate, microtubules and integrins. Myo10 also undergoes fascinating long-range movements within filopodia, which appear to represent a newly recognized system of transport. Myo10 is also unusual in that it is a myosin with important roles in the spindle, a microtubule-based structure. Exciting new studies have begun to reveal the structure and single-molecule properties of this intriguing myosin, as well as its mechanisms of regulation and induction of filopodia. At the cellular and organismal level, growing evidence demonstrates that Myo10 has crucial functions in numerous processes ranging from invadopodia formation to cell migration.
引用
收藏
页码:3733 / 3741
页数:9
相关论文
共 95 条
[1]   The Motor Protein Myosin-X Transports VE-Cadherin along Filopodia To Allow the Formation of Early Endothelial Cell-Cell Contacts [J].
Almagro, Sebastien ;
Durmort, Claire ;
Chervin-Petinot, Adeline ;
Heyraud, Stephanie ;
Dubois, Mathilde ;
Lambert, Olivier ;
Maillefaud, Camille ;
Hewat, Elizabeth ;
Schaal, Jean Patrick ;
Huber, Philippe ;
Gulino-Debrac, Danielle .
MOLECULAR AND CELLULAR BIOLOGY, 2010, 30 (07) :1703-1717
[2]   Ena/VASP proteins have an anti-capping, independent function in filopodia formation [J].
Applewhite, Derek A. ;
Barzik, Melanie ;
Kojima, Shin-ichiro ;
Svitkina, Tatyana M. ;
Gertler, Frank B. ;
Borisy, Gary G. .
MOLECULAR BIOLOGY OF THE CELL, 2007, 18 (07) :2579-2591
[3]  
Baboolal TG, 2009, P NATL ACAD SCI USA, V106, P22193, DOI [10.1073/pnas.0909851106, 10.1073/pnas.09098S1106]
[4]   Myosin-XVa is required for tip localization of whirlin and differential elongation of hair-cell stereocilia [J].
Belyantseva, IA ;
Boger, ET ;
Naz, S ;
Frolenkov, GI ;
Sellers, JR ;
Ahmed, ZM ;
Griffith, AJ ;
Friedman, TB .
NATURE CELL BIOLOGY, 2005, 7 (02) :148-U60
[5]   Interaction with the IQ3 motif of myosin-10 is required for calmodulin-like protein-dependent filopodial extension [J].
Bennett, Richard D. ;
Caride, Ariel J. ;
Mauer, Amy S. ;
Strehler, Emanuel E. .
FEBS LETTERS, 2008, 582 (16) :2377-2381
[6]   Calmodulin-like protein enhances myosin-10 translation [J].
Bennett, Richard D. ;
Strehler, Emanuel E. .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2008, 369 (02) :654-659
[7]   Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10 [J].
Bennett, Richard D. ;
Mauer, Amy S. ;
Strehler, Emanuel E. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (05) :3205-3212
[8]  
Berg JS, 2000, J CELL SCI, V113, P3439
[9]   Myosin-X is an unconventional myosin that undergoes intrafilopodial motility [J].
Berg, JS ;
Cheney, RE .
NATURE CELL BIOLOGY, 2002, 4 (03) :246-250
[10]   Myosin-X is a molecular motor that functions in filopodia formation [J].
Bohil, Aparna B. ;
Robertson, Brian W. ;
Cheney, Richard E. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (33) :12411-12416