Cenp-F Links Kinetochores to Ndel1/Nde1/Lis1/Dynein Microtubule Motor Complexes

Maïlys A S Vergnolle, Stephen S. Taylor

    Research output: Contribution to journalArticlepeer-review


    Cenp-F is a nuclear matrix component that localizes to kinetochores during mitosis and is then rapidly degraded after mitosis [1]. Unusually, both the localization and degradation of Cenp-F require it to be farnesylated [2]. Five studies recently demonstrated that Cenp-F is required for kinetochore-microtubule interactions and spindle checkpoint function [3-7]; however, the underlying molecular mechanisms have yet to be defined. Here, we show that Cenp-F interacts with Ndel1 and Nde1, two human NudE-related proteins implicated in regulating Lis1/Dynein motor complexes (reviewed in [8]). We show that Ndel1, Nde1, and Lis1 localize to kinetochores in a Cenp-F-dependent manner. In addition, Nde1, but not Ndel1, is required for kinetochore localization of Dynein. Accordingly, suppression of Nde1 inhibits metaphase chromosome alignment and activates the spindle checkpoint. By contrast, inhibition of Ndel1 results in malorientations that are not detected by the spindle checkpoint; Ndel1-deficient cells consequently enter anaphase in a timely manner but lagging chromosomes then manifest. A major function of Cenp-F, therefore, is to link the Ndel1/Nde1/Lis1/Dynein pathway to kinetochores. Furthermore, our data demonstrate that Ndel1 and Nde1 play distinct roles to ensure chromosome alignment and segregation. © 2007 Elsevier Ltd. All rights reserved.
    Original languageEnglish
    Pages (from-to)1173-1179
    Number of pages6
    JournalCurrent Biology
    Issue number13
    Publication statusPublished - 3 Jul 2007




    Dive into the research topics of 'Cenp-F Links Kinetochores to Ndel1/Nde1/Lis1/Dynein Microtubule Motor Complexes'. Together they form a unique fingerprint.

    Cite this