Luna Lab Publications

UMMS Affiliation

Department of Cell and Developmental Biology; Program in Cell and Developmental Dynamics

Date

12-1-2013

Document Type

Article

Disciplines

Cell Biology

Abstract

Cytokinesis, the process in which cytoplasm is apportioned between dividing daughter cells, requires coordination of myosin II function, membrane trafficking and central spindle organization. Most known regulators act during late cytokinesis; a few, including the myosin II-binding proteins anillin and supervillin, act earlier. Anillin's role in scaffolding the membrane cortex with the central spindle is well established, but the mechanism of supervillin action is relatively uncharacterized. We show here that two regions within supervillin affect cell division: residues 831-1281, which bind central spindle proteins, and residues 1-170, which bind the myosin II heavy chain (MHC) and the long form of myosin light chain kinase (l-MLCK). MHC binding is required to rescue supervillin deficiency, and mutagenesis of this site creates a dominant-negative phenotype. Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin additively increase cell division failure. Knockdown of either protein causes mislocalization of the other, and endogenous anillin increases upon supervillin knockdown. Proteomic identification of interaction partners recovered using a high-affinity GFP nanobody suggest that supervillin and anillin regulate the myosin II- and actin cortical cytoskeletons through separate pathways. We conclude that supervillin and anillin play complementary roles during vertebrate cytokinesis.

Comments

Citation: Smith TC, Fridy PC, Li Y, Basil S, Arjun S, Friesen RM, Leszyk J, Chait BT, Rout MP, Luna EJ. Supervillin binding to myosin II and synergism with anillin are required for cytokinesis. Mol Biol Cell. 2013 Dec;24(23):3603-19. doi:10.1091/mbc.E12-10-0714. Link to article from publisher's site

© 2013 Smith et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

Publisher PDF posted as allowed by the publisher's author rights policy at http://www.molbiolcell.org/site/misc/ifora.xhtml.

Related Resources

Link to article in PubMed

Keywords

Cytokinesis, Cell division, Supervillin, Myosin, Anillin

PubMed ID

24088567

Included in

Cell Biology Commons

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