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First published online 28 September 2004
doi: 10.1242/jcs.01389

Journal of Cell Science 117, 5313-5321 (2004)
Published by The Company of Biologists 2004
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Research Article

Maternal UNC-45 is involved in cytokinesis and colocalizes with non-muscle myosin in the early Caenorhabditis elegans embryo

Torah Kachur*, Wanyuan Ao*,{ddagger}, Jeffrey Berger§ and Dave Pilgrim

Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, T6G 2E9, Canada

Author for correspondence (e-mail: dave.pilgrim{at}ualberta.ca)

Accepted 28 June 2004

The Caenorhabditis elegans UNC-45 protein contains tetratricopeptide repeats and a domain with similarity to fungal proteins, and it differentially colocalizes with myosin heavy chain B in the body wall muscles of adult worms. Although it is essential for normal myosin filament assembly in body wall muscle development, strong mutants show a previously unexplained maternal effect. We show here that the UNC-45 protein is maternally contributed and is present in all cells of the early embryo whereas zygotic UNC-45 expression is only detected in the developing muscle cells. Embryos produced from adults with reduced germline expression of UNC-45 exhibit cytokinesis defects suggesting that UNC-45 has a novel role in the early embryo in addition to muscle development. Yeast two-hybrid screens show that UNC-45 can directly interact with NMY-2, a non-muscle type II myosin, and UNC-45 and NMY-2 colocalize at cell boundaries in early embryos. Localization of UNC-45 at these boundaries is dependent upon the presence of NMY-2. Our results suggest that UNC-45 interacts with more than one type of myosin and functions in the embryo to regulate cytoplasmic myosin assembly and/or stability during cytokinesis.

Key words: Myosin heavy chain, UCS domain protein, Cytokinesis, Two-hybrid assay, Non-muscle myosin




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