TY - JOUR
T1 - A postmitotic function and distinct localization mechanism for centralspindlin at a stable intercellular bridge
AU - Zhou, Kang
AU - Rolls, Melissa M.
AU - Hanna-Rose, Wendy
N1 - Funding Information:
We would like to thank Julie C. Canman and Bruce E. Vogel for sharing C. elegans strains and Karen Oegema for the ANI-2 antibody. Some nematode strains used in this work were provided by the Caenorhabditis elegans Genetics Center, which is funded by the NIH National Center for Research Resources (NCRR) . MMR is a Pew Scholar in the Biomedical Sciences. This work was supported in part by a grant to W.H-R. from the National Science Foundation (IOS- 0718675 ).
PY - 2013/4/1
Y1 - 2013/4/1
N2 - Centralspindlin, a complex composed of the subunits ZEN-4 and CYK-4, recruits and regulates proteins that modulate the actin cytoskeleton to promote cleavage furrow formation and progression during cytokinesis. The ZEN-4 subunit is a kinesin that is proposed to function primarily by bundling microtubules and promoting transport of the complex to the midzone. ZEN-4 and CYK-4 are mutually dependent for localization to the midzone during cytokinesis. Once at the midzone, the CYK-4 subunit functions to recruit actin regulators and the scaffold anillin as well as to regulate RhoA and Rac via its intrinsic GAP domain, ultimately promoting actomyosin contractile ring assembly. We have revealed a distinct mechanism for centralspindlin localization and function at a stable, postmitotic intercellular bridge in the Caenorhabditis elegans gonad. Loss of zen-4 or cyk-4 function disrupts germ cell progression postmitotically. In contrast to the localization and recruitment relationships during mitosis, centralspindlin is maintained at the intercellular bridge by anillin, and CYK-4 is localized independently of ZEN-4 but not vice versa. We present evidence that centralspindlin function at the rachis bridge involves ZEN-4 action on the microtubules as opposed to the regulation of the actin cytoskeleton mediated by CYK-4 during cytokinesis.
AB - Centralspindlin, a complex composed of the subunits ZEN-4 and CYK-4, recruits and regulates proteins that modulate the actin cytoskeleton to promote cleavage furrow formation and progression during cytokinesis. The ZEN-4 subunit is a kinesin that is proposed to function primarily by bundling microtubules and promoting transport of the complex to the midzone. ZEN-4 and CYK-4 are mutually dependent for localization to the midzone during cytokinesis. Once at the midzone, the CYK-4 subunit functions to recruit actin regulators and the scaffold anillin as well as to regulate RhoA and Rac via its intrinsic GAP domain, ultimately promoting actomyosin contractile ring assembly. We have revealed a distinct mechanism for centralspindlin localization and function at a stable, postmitotic intercellular bridge in the Caenorhabditis elegans gonad. Loss of zen-4 or cyk-4 function disrupts germ cell progression postmitotically. In contrast to the localization and recruitment relationships during mitosis, centralspindlin is maintained at the intercellular bridge by anillin, and CYK-4 is localized independently of ZEN-4 but not vice versa. We present evidence that centralspindlin function at the rachis bridge involves ZEN-4 action on the microtubules as opposed to the regulation of the actin cytoskeleton mediated by CYK-4 during cytokinesis.
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U2 - 10.1016/j.ydbio.2013.01.020
DO - 10.1016/j.ydbio.2013.01.020
M3 - Article
C2 - 23370148
AN - SCOPUS:84875388642
SN - 0012-1606
VL - 376
SP - 13
EP - 22
JO - Developmental biology
JF - Developmental biology
IS - 1
ER -