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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

Authors :
Joseph S. Wolenski
Foued Salmen Espindola
Daniel M. Suter
Leticia B.E. Partata
Richard E. Cheney
Stephen M. King
Tracy T. Cao
Mark S. Mooseker
Source :
Cell Motility and the Cytoskeleton. 47:269-281
Publication Year :
2000
Publisher :
Wiley, 2000.

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 Ca(2+) 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.

Details

ISSN :
10970169 and 08861544
Volume :
47
Database :
OpenAIRE
Journal :
Cell Motility and the Cytoskeleton
Accession number :
edsair.doi...........a0799c61576323ab47c359ee9806c2ee
Full Text :
https://doi.org/10.1002/1097-0169(200012)47:4<269::aid-cm2>3.0.co;2-g