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PMID: 21173112 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Biphasic targeting and cleavage furrow ingression directed by the tail of a myosin II.

The Journal of cell biology ·Vol. 191 ·No. 7 ·2010-12-27 ·Pages 1333-50

Fang X, Luo J, Nishihama R, Wloka C, Dravis C, Travaglia M, Iwase M, Vallen EA, Bi E

Abstract

Cytokinesis in animal and fungal cells utilizes a contractile actomyosin ring (AMR). However, how myosin II is targeted to the division site and promotes AMR assembly, and how the AMR coordinates with membrane trafficking during cytokinesis, remains poorly understood. Here we show that Myo1 is a two-headed myosin II in Saccharomyces cerevisiae, and that Myo1 localizes to the division site via two distinct targeting signals in its tail that act sequentially during the cell cycle. Before cytokinesis, Myo1 localization depends on the septin-binding protein Bni5. During cytokinesis, Myo1 localization depends on the IQGAP Iqg1. We also show that the Myo1 tail is sufficient for promoting the assembly of a "headless" AMR, which guides membrane deposition and extracellular matrix remodeling at the division site. Our study establishes a biphasic targeting mechanism for myosin II and highlights an underappreciated role of the AMR in cytokinesis beyond force generation.

MeSH Terms
Actin Cytoskeleton/metabolism Actins/metabolism Actomyosin/metabolism Cell Cycle/physiology Cytokinesis/physiology Kinetics Myosin Heavy Chains/genetics,metabolism,ultrastructure Myosin Light Chains/genetics Myosin Subfragments/genetics,metabolism,ultrastructure Protein Binding/physiology Protein Interaction Domains and Motifs/physiology Protein Structure, Quaternary Protein Transport/physiology Recombinant Fusion Proteins/genetics,metabolism,ultrastructure Saccharomyces cerevisiae/physiology Saccharomyces cerevisiae Proteins/genetics,metabolism,ultrastructure ras GTPase-Activating Proteins/genetics
Chemicals
Actins BNI5 protein, S cerevisiae IQ motif containing GTPase activating protein 1 MLC1 protein, S cerevisiae MYO1 protein, S cerevisiae Myosin Light Chains Myosin Subfragments Recombinant Fusion Proteins Saccharomyces cerevisiae Proteins ras GTPase-Activating Proteins Actomyosin Myosin Heavy Chains
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Fang Xiaodong
Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
Luo Jianying
Nishihama Ryuichi
Wloka Carsten
Dravis Christopher
Travaglia Mirko
Iwase Masayuki
Vallen Elizabeth A
Bi Erfei
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
1540-8140
Published
2010-12-27
Epub
2010-00-20
Pages
1333-50
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC3010076
Subset
IM
Grants
NIAMS NIH HHS · P01 AR051174 · United States
NIGMS NIH HHS · R01 GM059216 · United States
NIGMS NIH HHS · R37 GM031006 · United States
NIGMS NIH HHS · GM31006 · United States
NIGMS NIH HHS · R01 GM031006 · United States
NIAMS NIH HHS · P01-AR051174 · United States
NIGMS NIH HHS · GM59216 · United States
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