UNC-45 is required for NMY-2 contractile function in early embryonic polarity establishment and germline cellularization in C. elegans

Dev Biol. 2008 Feb 15;314(2):287-99. doi: 10.1016/j.ydbio.2007.11.028. Epub 2007 Dec 4.


The Caenorhabditis elegans UNC-45 protein is required for proper body wall muscle assembly and acts as a molecular co-chaperone for type II myosins. In contrast to other body wall muscle components, UNC-45 is also abundant in the germline and embryo. We show that maternally provided UNC-45 acts with non-muscle myosin II (NMY-2) during embryonic polarity establishment, cytokinesis and germline cellularization. In embryos depleted for UNC-45, myosin contractility is eliminated resulting in embryonic defects in polar body extrusion, cytokinesis and establishment of polarity. Despite a lack of contractility in an unc-45(RNAi) embryo, NMY-2::GFP localizes to the cortex and accumulates at the presumptive cytokinetic furrow indicating that UNC-45 is not required for cortical localization. UNC-45 and NMY-2 are also required for fertility since the lack of either component results in complete sterility due to failed initiation of the cellularization furrows that separate syncytial nuclei into germ cells. In the absence of UNC-45, the actomyosin cytoskeleton does not contract despite non-functional myosin still directly binding actin. UNC-45 has been previously suggested to be required for the folding of the myosin head, and our results refine this hypothesis suggesting that UNC-45 is not required to fold or maintain the actin binding domain but is still required for myosin function.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Animals
  • Body Patterning / physiology
  • Caenorhabditis elegans / cytology
  • Caenorhabditis elegans / embryology*
  • Caenorhabditis elegans Proteins / physiology*
  • Embryo, Nonmammalian / physiology*
  • Embryonic Development / physiology
  • Infertility
  • Infertility, Male
  • Male
  • Molecular Chaperones / physiology*
  • Muscle Contraction
  • Myosin Heavy Chains / physiology*
  • Myosins / metabolism
  • Myosins / physiology
  • Protein Folding
  • RNA Interference*
  • Spermatozoa / physiology*


  • Actins
  • Caenorhabditis elegans Proteins
  • Molecular Chaperones
  • NMY-2 protein, C elegans
  • unc-45 protein, C elegans
  • Myosin Heavy Chains
  • Myosins