4.7 Article

The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex

Journal

JOURNAL OF CELL BIOLOGY
Volume 202, Issue 2, Pages 251-260

Publisher

ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201304052

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Funding

  1. Fonds de Recherche du Quebec en Sante (FRQS) fellowship
  2. National Institutes of Health [R01GM086536]
  3. Canadian Institutes of Health Research (CIHR) [MOP-89877, MOP-97928]
  4. Natural Sciences and Engineering Research Council of Canada
  5. Canadian Center of Excellence in Commercialization and Research
  6. Canada Foundation for Innovation
  7. Canada Foundation for Innovation, and by the FRQS

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Ezrin, Radixin, and Moesin (ERM) proteins play important roles in many cellular processes including cell division. Recent studies have highlighted the implications of their metastatic potential in cancers. ERM's role in these processes is largely attributed to their ability to link actin filaments to the plasma membrane. In this paper, we show that the ERM protein Moesin directly binds to microtubules in vitro and stabilizes microtubules at the cell cortex in vivo. We identified two evolutionarily conserved residues in the FERM (4.1 protein and ERM) domains of ERMs that mediated the association with microtubules. This ERM-microtubule interaction was required for regulating spindle organization in metaphase and cell shape transformation after anaphase onset but was dispensable for bridging actin filaments to the metaphase cortex. These findings provide a molecular framework for understanding the complex functional interplay between the microtubule and actin cytoskeletons mediated by ERM proteins in mitosis and have broad implications in both physiological and pathological processes that require ERMs.

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