title: The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex.
abstract: 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.
authors.affiliation: Cellular Mechanisms of Morphogenesis during Mitosis and Cell Motility, Université de Montréal, Montréal, Québec H3C 3J7, Canada.
authors.forename: Sara
authors.initials: S
authors.lastname: Solinet
authors.forename: Kazi
authors.initials: K
authors.lastname: Mahmud
authors.forename: Shannon F
authors.initials: SF
authors.lastname: Stewman
authors.forename: Khaled
authors.initials: K
authors.lastname: Ben El Kadhi
authors.forename: Barbara
authors.initials: B
authors.lastname: Decelle
authors.forename: Lama
authors.initials: L
authors.lastname: Talje
authors.forename: Ao
authors.initials: A
authors.lastname: Ma
authors.forename: Benjamin H
authors.initials: BH
authors.lastname: Kwok
authors.forename: Sébastien
authors.initials: S
authors.lastname: Carreno
mesh_terms: D008841:Actin Cytoskeleton / Q000235:genetics / Q000378:metabolism*; D000705:Anaphase; D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D003001:Cloning, Molecular; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D004330:Drosophila / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007399:Interphase; D008164:Luminescent Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008677:Metaphase; D008870:Microtubules / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000378:metabolism; D008941:Spindle Apparatus / Q000235:genetics / Q000378:metabolism; D000097573:Red Fluorescent Protein; D000099149:Ezrin
chemical_list: D003598:Cytoskeletal Proteins; D008164:Luminescent Proteins; D008565:Membrane Proteins; D011994:Recombinant Proteins; D000097573:Red Fluorescent Protein; D000099149:Ezrin; C099886:moesin, Drosophila