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Enhancement of myosin II / actin turnover at the contractile ring induces slower furrowing in dividing HeLa cells.
MedLine Citation:
PMID:  21231914     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Myosin II ATPase activity is enhanced by the phosphorylation of its regulatory light chain (MRLC) in non-muscle cells. It is well known that phosphorylated MRLC (P-MRLC) colocalizes with F-actin in the contractile ring (CR) of dividing cells. Recently, we reported that HeLa cells expressing non-phosphorylatable MRLC show a delay in the speed of furrow ingression, suggesting that P-MRLC plays an important role in the control of furrow ingression. However, it is still unclear how P-MRLC regulates myosin II and F-actin at the CR to control furrow ingression during cytokinesis. Here, to clarify the roles of P-MRLC, we measured the turnover of myosin II and actin at the CR in dividing HeLa cells expressing fluorescent-tagged MRLCs and actin by fluorescence recovery after photobleaching. A myosin II inhibitor, blebbistatin, caused an enhancement of the turnover of MRLC and actin at the CR, which induced a delay of furrow ingression. Furthermore, only non-phosphorylatable MRLC and a Rho-kinase inhibitor, Y-27632, accelerated the turnover of MRLC and actin at the CR. Interestingly, the effect of Y-27632 was cancelled in the cell expressing phospho-mimic MRLCs. Taken together, these data reveal that P-MRLC reduces the turnover of myosin II and also actin at the CR. In conclusion, we show that the enhancement of myosin II and actin turnover at the CR induced slower furrowing in dividing HeLa cells.
Authors:
Tomo Kondo; Kozue Hamao; Keiju Kamijo; Hiroshi Kimura; Makiko Morita; Hiroshi Hosoya
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-1-13
Journal Detail:
Title:  The Biochemical journal     Volume:  -     ISSN:  1470-8728     ISO Abbreviation:  -     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-1-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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