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Published 15 August 2005. doi:10.1083/jcb.200501097
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 4, 571-582
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Article

An ECT2–centralspindlin complex regulates the localization and function of RhoA



Özlem Yüce, Alisa Piekny, and Michael Glotzer

Research Institute of Molecular Pathology, 1030 Vienna, Austria

Correspondence to Michael Glotzer: mglotzer{at}uchicago.edu

In anaphase, the spindle dictates the site of contractile ring assembly. Assembly and ingression of the contractile ring involves activation of myosin-II and actin polymerization, which are triggered by the GTPase RhoA. In many cells, the central spindle affects division plane positioning via unknown molecular mechanisms. Here, we dissect furrow formation in human cells and show that the RhoGEF ECT2 is required for cortical localization of RhoA and contractile ring assembly. ECT2 concentrates on the central spindle by binding to centralspindlin. Depletion of the centralspindlin component MKLP1 prevents central spindle localization of ECT2; however, RhoA, F-actin, and myosin still accumulate on the equatorial cell cortex. Depletion of the other centralspindlin component, CYK-4/MgcRacGAP, prevents cortical accumulation of RhoA, F-actin, and myosin. CYK-4 and ECT2 interact, and this interaction is cell cycle regulated via ECT2 phosphorylation. Thus, central spindle localization of ECT2 assists division plane positioning and the CYK-4 subunit of centralspindlin acts upstream of RhoA to promote furrow assembly.

Ö. Yüce and A. Piekny contributed equally to this paper.

A. Piekny and M. Glotzer's present address is Dept. of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637.

Abbreviations used in this paper: BRCT, BRCA1 COOH terminus; CBD, chitin binding domain; GAP, GTPase activating protein; GEF, guanine nucleotide exchange factor; LatA, Latrunculin A.


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