Published in
Wiley, Cell Motility and the Cytoskeleton, 4(47), p. 269-281, 2000
DOI: 10.1002/1097-0169(200012)47:4<269::aid-cm2>3.0.co;2-g
Wiley, Cell Motility and the Cytoskeleton, 4(47), p. 269-281
DOI: 10.1002/1097-0169(200012)47:4<269::aid-cm2>3.3.co;2-7
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The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN
,
Espindola Fs,
Daniel M. Suter,
Suter Dm,
Partata Lb,
Leticia B. E. Partata,
Tracy Cao,
Joseph S. Wolenski,
Wolenski Js,
Richard E. Cheney,
Cheney Re,
Stephen M. King,
Mark S. Mooseker,
King Sm,
Mooseker Ms
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Abstract
Class V myosins are a ubiquitously expressed family of actin-based molecular motors. Biochemical studies on myosin-Va from chick brain indicate that this myosin is a two-headed motor with multiple calmodulin light chains associated with the regulatory or neck domain of each heavy chain, a feature consistent with the regulatory effects of Ca2+ on this myosin. In this study, the identity of three additional low molecular weight proteins of 23-,17-, and 10 kDa associated with myosin-Va is established. The 23- and 17-kDa subunits are both members of the myosin-II essential light chain gene family, encoded by the chicken L23 and L17 light chain genes, respectively. The 10-kDa subunit is a protein originally identified as a light chain (DLC8) of flagellar and axonemal dynein. The 10-kDa subunit is associated with the tail domain of myosin-Va. Cell Motil. Cytoskeleton 47:269–281, 2000. © 2000 Wiley-Liss, Inc.