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

被引:61
作者
Kachur, Torah M. [1 ]
Audhya, Anjon [2 ]
Pilgrim, Dave B. [1 ]
机构
[1] Univ Alberta, Dept Biol Sci, Edmonton, AB T6G 2E9, Canada
[2] Univ Calif San Diego, Dept Cellular & Mol Med, Ludwig Inst Canc Res, La Jolla, CA 92093 USA
关键词
embryonic polarity; UNC-45; gemiline cellularization; myosin; NMY-2; chaperone;
D O I
10.1016/j.ydbio.2007.11.028
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:287 / 299
页数:13
相关论文
共 57 条
[1]  
[Anonymous], 1988, NEMATODE CAENORHABDI
[2]   Caenorhabditis elegans UNC-45 is a component of muscle thick filaments and colocalizes with myosin heavy chain B, but not myosin heavy chain A [J].
Ao, WY ;
Pilgrim, D .
JOURNAL OF CELL BIOLOGY, 2000, 148 (02) :375-384
[3]   Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly [J].
Barral, JM ;
Bauer, CC ;
Ortiz, I ;
Epstein, HF .
JOURNAL OF CELL BIOLOGY, 1998, 143 (05) :1215-1225
[4]   Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin [J].
Barral, JM ;
Hutagalung, AH ;
Brinker, A ;
Hartl, FU ;
Epstein, HF .
SCIENCE, 2002, 295 (5555) :669-671
[5]   Myosin II co-chaperone general cell UNC-45 overexpression is associated with ovarian cancer, rapid proliferation, and motility [J].
Bazzaro, Martina ;
Santillan, Antonio ;
Lin, Zhenhua ;
Tang, Taylor ;
Lee, Michael K. ;
Bristow, Robert E. ;
Shih, Le-Ming ;
Roden, Richard B. S. .
AMERICAN JOURNAL OF PATHOLOGY, 2007, 171 (05) :1640-1649
[6]   A homologue of the yeast SHE4 gene is essential for the transition between the syncytial and cellular stages during sexual reproduction of the fungus Podospora anserina [J].
Berteaux-Lecellier, V ;
Zickler, D ;
Debuchy, R ;
Panvier-Adoutte, A ;
Thompson-Coffe, C ;
Picard, M .
EMBO JOURNAL, 1998, 17 (05) :1248-1258
[7]   Folding of the striated muscle myosin motor domain [J].
Chow, D ;
Srikakulam, R ;
Chen, Y ;
Winkelmann, DA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (39) :36799-36807
[8]   Acto-myosin reorganization and PAR polarity in C-elegans [J].
Cowan, Carrie R. ;
Hyman, Anthony A. .
DEVELOPMENT, 2007, 134 (06) :1035-1043
[9]   Polarization of the C-elegans zygote proceeds via distinct establishment and maintenance phases [J].
Cuenca, AA ;
Schetter, A ;
Aceto, D ;
Kemphues, K ;
Seydoux, G .
DEVELOPMENT, 2003, 130 (07) :1255-1265
[10]   TEMPERATURE-SENSITIVE MUTATION AFFECTING MYOFILAMENT ASSEMBLY IN CAENORHABDITIS-ELEGANS [J].
EPSTEIN, HF ;
THOMSON, JN .
NATURE, 1974, 250 (5467) :579-580