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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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.