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Published online
doi:10.1083/jcb.200903125
The Journal of Cell Biology, Vol. 185, No. 6, 995-1012
The Rockefeller University Press, 0021-9525 $30.00
© Nishihama et al.
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Article

Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae



Ryuichi Nishihama1, Jennifer H. Schreiter2, Masayuki Onishi1, Elizabeth A. Vallen4, Julia Hanna2, Katarina Moravcevic3, Margaret F. Lippincott4, Haesun Han4, Mark A. Lemmon3, John R. Pringle1, and Erfei Bi2

1 Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305
2 Department of Cell and Developmental Biology and 3 Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104
4 Department of Biology, Swarthmore College, Swarthmore, PA 19081

Correspondence to Erfei Bi: ebi{at}mail.med.upenn.edu

Cytokinesis requires coordination of actomyosin ring (AMR) contraction with rearrangements of the plasma membrane and extracellular matrix. In Saccharomyces cerevisiae, new membrane, the chitin synthase Chs2 (which forms the primary septum [PS]), and the protein Inn1 are all delivered to the division site upon mitotic exit even when the AMR is absent. Inn1 is essential for PS formation but not for Chs2 localization. The Inn1 C-terminal region is necessary for localization, and distinct PXXP motifs in this region mediate functionally important interactions with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore PS formation in inn1{Delta} cells). The Inn1 N terminus resembles C2 domains but does not appear to bind phospholipids; nonetheless, when overexpressed or fused to Hof1, it can provide Inn1 function even in the absence of the AMR. Thus, Inn1 and Cyk3 appear to cooperate in activating Chs2 for PS formation, which allows coordination of AMR contraction with ingression of the cleavage furrow.

R. Nishihama, J.H. Schreiter, M. Onishi, and E.A. Vallen contributed equally to this paper.

Abbreviations used in this paper: AD, activation domain; AMR, actomyosin ring; CCD, charge-coupled device; DBD, DNA-binding domain; DIC, differential interference contrast; FOA, 5-fluoroorotic acid; latA, latrunculin A; MEN, mitotic exit network; PS, primary septum; SPR, surface plasmon resonance; SS, secondary septum; TAP, tandem affinity purification; TEM, transmission EM.

© 2009 Nishihama et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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