Please use this identifier to cite or link to this item: https://doi.org/10.1083/jcb.200402097
DC FieldValue
dc.titleMyosin-II reorganization during mitosis is controlled temporally by its dephosphorylation spatially by Mid1 in fission yeast
dc.contributor.authorMotegi, F.
dc.contributor.authorMishra, M.
dc.contributor.authorBalasubramanian, M.K.
dc.contributor.authorMabuchi, I.
dc.date.accessioned2016-12-19T06:49:50Z
dc.date.available2016-12-19T06:49:50Z
dc.date.issued2004-06-07
dc.identifier.citationMotegi, F., Mishra, M., Balasubramanian, M.K., Mabuchi, I. (2004-06-07). Myosin-II reorganization during mitosis is controlled temporally by its dephosphorylation spatially by Mid1 in fission yeast. Journal of Cell Biology 165 (5) : 685-695. ScholarBank@NUS Repository. https://doi.org/10.1083/jcb.200402097
dc.identifier.issn00219525
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/133348
dc.description.abstractCytokinesis in many eukaryotes requires an actomyosin contractile ring. Here, we show that in fission yeast the myosin-II heavy chain Myo2 initially accumulates at the division site via its COOH-terminal 134 amino acids independently of F-actin. The COOH-terminal region can access to the division site at early G2, whereas intact Myo2 does so at early mitosis. Ser1444 in the Myo2 COOH-terminal region is a phosphorylation site that is dephosphorylated during early mitosis. Myo2 S1444A prematurely accumulates at the future division site and promotes formation of an F-actin ring even during interphase. The accumulation of Myo2 requires the anillin homologue Mid1 that functions in proper ring placement. Myo2 interacts with Mid1 in cell lysates, and this interaction is inhibited by an S1444D mutation in Myo2. Our results suggest that dephosphorylation of Myo2 liberates the COOH-terminal region from an intramolecular inhibition. Subsequently, dephosphorylated Myo2 is anchored by Mid1 at the medial cortex and promotes the ring assembly in cooperation with F-actin.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1083/jcb.200402097
dc.sourceScopus
dc.subjectActin
dc.subjectContractile ring
dc.subjectCytokinesis
dc.subjectMyosin
dc.subjectPhosphorylation
dc.typeArticle
dc.contributor.departmentTEMASEK LABORATORIES
dc.description.doi10.1083/jcb.200402097
dc.description.sourcetitleJournal of Cell Biology
dc.description.volume165
dc.description.issue5
dc.description.page685-695
dc.description.codenJCLBA
dc.identifier.isiut000221986200010
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

104
checked on Feb 3, 2023

WEB OF SCIENCETM
Citations

101
checked on Feb 3, 2023

Page view(s)

122
checked on Feb 2, 2023

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.