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. 2008 Dec 1;183(5):819–834. doi: 10.1083/jcb.200804114

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© 2008 Whyte 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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Figure 9. — New model for regulation of cytoplasmic dynein at kinetochores. During prometaphase, dynein is loaded onto kinetochores via binding of phosphodynein to zw10 (t = 1). As MTs attach to kinetochores and chromosomes congress to the metaphase plate (t = 2), dynein undergoes dephosphorylation, shifting binding from zw10 to dynactin (t = 2). This transition stimulates dynein for translocation away from kinetochores (t = 3). Because activated dynein contributes to the removal of anaphase inhibitors from kinetochores, dynein dephosphorylation reduces the ability of kinetochores to produce active anaphase inhibitors.