A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Franke, J.D., Boury, A.L., Gerald, N.J., Kiehart, D.P. (2006). Native nonmuscle myosin II stability and light chain binding in Drosophila melanogaster.  Cell Motility Cytoskel. 63(10): 604--622. (Export to RIS)
FlyBase ID FBrf0193420
Publication Type Research paper
PubMed ID 16917818
PubMed Abstract Native nonmuscle myosin IIs play essential roles in cellular and developmental processes throughout phylogeny. Individual motor molecules consist of a heterohexameric complex of three polypeptides which, when properly assembled, are capable of force generation. Here, we more completely characterize the properties, relationships and associations that each subunit has with one another in Drosophila melanogaster. All three native nonmuscle myosin II polypeptide subunits are expressed in close to constant stoichiometry to each other throughout development. We find that the stability of two subunits, the heavy chain and the regulatory light chain, depend on one another whereas the stability of the third subunit, the essential light chain, does not depend on either the heavy chain or regulatory light chain. We demonstrate that heavy chain aggregates, which form when regulatory light chain is lacking, associate with the essential light chain in vivo-thus showing that regulatory light chain association is required for heavy chain solubility. By immunodepletion we find that the majority of both light chains are associated with the nonmuscle myosin II heavy chain but pools of free light chain and/or light chain bound to other proteins are present. We identify four myosins (myosin II, myosin V, myosin VI and myosin VIIA) and a microtubule-associated protein (asp/Abnormal spindle) as binding partners for the essential light chain (but not the regulatory light chain) through mass spectrometry and co-precipitation. Using an in silico approach we identify six previously uncharacterized genes that contain IQ-motifs and may be essential light chain binding partners.
DOI 10.1002/cm.20148
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Language of Publication English
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Publication Type Journal
Abbreviation Cell Motility Cytoskel.
Title Cell Motility and the Cytoskeleton
Publication Year 1986-
ISBN/ISSN 0886-1544
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