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Direct evidence for roles of phosphorylated regulatory light chain of myosin II in furrow ingression during cytokinesis in HeLa cells.
Genes Cells 2009; 14(5):555-68GC

Abstract

Phosphorylation of myosin II is thought to play an important role in cytokinesis. Although it is well known that phosphorylated regulatory light chain of myosin II (P-MRLC) localizes along the contractile ring, it is not clear how P-MRLC controls myosin II and F-actin in furrow ingression during cytokinesis. To elucidate roles of P-MRLC in furrow ingression, HeLa cells transfected with EGFP-tagged wild-type or each MRLC mutant were observed using a live-imaging microscope. Time-lapse observation revealed that a delay of furrow ingression was observed in the nonphosphorylatable form of MRLC (AA-MRLC)-expressing cell but not in the wild-type or phospho-mimic MRLC-expressing cell. Among each form of MRLC-expressing cell, the total amount of P-MRLC including phospho-mimic MRLCs was smallest in the cell expressing AA-MRLC. However, the amount of F-actin and myosin II at the contractile ring in the AA-MRLC-expressing cell was the same as that in the normal cell. Interestingly, delay of furrow ingression by a Rho-kinase inhibitor, Y27632, was rescued by phospho-mimic MRLCs. These results suggest that the P-MRLC is essential for the progress of furrow ingression but not the retainment of F-actin and myosin II in the contractile ring of dividing HeLa cells.

Authors+Show Affiliations

Department of Biological Science, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

19371382

Citation

Asano, Satoshi, et al. "Direct Evidence for Roles of Phosphorylated Regulatory Light Chain of Myosin II in Furrow Ingression During Cytokinesis in HeLa Cells." Genes to Cells : Devoted to Molecular & Cellular Mechanisms, vol. 14, no. 5, 2009, pp. 555-68.
Asano S, Hamao K, Hosoya H. Direct evidence for roles of phosphorylated regulatory light chain of myosin II in furrow ingression during cytokinesis in HeLa cells. Genes Cells. 2009;14(5):555-68.
Asano, S., Hamao, K., & Hosoya, H. (2009). Direct evidence for roles of phosphorylated regulatory light chain of myosin II in furrow ingression during cytokinesis in HeLa cells. Genes to Cells : Devoted to Molecular & Cellular Mechanisms, 14(5), pp. 555-68. doi:10.1111/j.1365-2443.2009.01288.x.
Asano S, Hamao K, Hosoya H. Direct Evidence for Roles of Phosphorylated Regulatory Light Chain of Myosin II in Furrow Ingression During Cytokinesis in HeLa Cells. Genes Cells. 2009;14(5):555-68. PubMed PMID: 19371382.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Direct evidence for roles of phosphorylated regulatory light chain of myosin II in furrow ingression during cytokinesis in HeLa cells. AU - Asano,Satoshi, AU - Hamao,Kozue, AU - Hosoya,Hiroshi, Y1 - 2009/04/15/ PY - 2009/4/18/entrez PY - 2009/4/18/pubmed PY - 2010/3/17/medline SP - 555 EP - 68 JF - Genes to cells : devoted to molecular & cellular mechanisms JO - Genes Cells VL - 14 IS - 5 N2 - Phosphorylation of myosin II is thought to play an important role in cytokinesis. Although it is well known that phosphorylated regulatory light chain of myosin II (P-MRLC) localizes along the contractile ring, it is not clear how P-MRLC controls myosin II and F-actin in furrow ingression during cytokinesis. To elucidate roles of P-MRLC in furrow ingression, HeLa cells transfected with EGFP-tagged wild-type or each MRLC mutant were observed using a live-imaging microscope. Time-lapse observation revealed that a delay of furrow ingression was observed in the nonphosphorylatable form of MRLC (AA-MRLC)-expressing cell but not in the wild-type or phospho-mimic MRLC-expressing cell. Among each form of MRLC-expressing cell, the total amount of P-MRLC including phospho-mimic MRLCs was smallest in the cell expressing AA-MRLC. However, the amount of F-actin and myosin II at the contractile ring in the AA-MRLC-expressing cell was the same as that in the normal cell. Interestingly, delay of furrow ingression by a Rho-kinase inhibitor, Y27632, was rescued by phospho-mimic MRLCs. These results suggest that the P-MRLC is essential for the progress of furrow ingression but not the retainment of F-actin and myosin II in the contractile ring of dividing HeLa cells. SN - 1365-2443 UR - https://www.unboundmedicine.com/medline/citation/19371382/Direct_evidence_for_roles_of_phosphorylated_regulatory_light_chain_of_myosin_II_in_furrow_ingression_during_cytokinesis_in_HeLa_cells_ L2 - https://doi.org/10.1111/j.1365-2443.2009.01288.x DB - PRIME DP - Unbound Medicine ER -