title: The actin-binding ERM protein Moesin directly regulates spindle assembly and function during mitosis.
abstract: Ezrin-Radixin-Moesin proteins are highly conserved, actin-binding cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis by linking actin filaments to the plasma membrane. Recent studies demonstrated that the only Ezrin-Radixin-Moesin protein of Drosophila melanogaster, Moesin, is involved in mitotic spindle function through stabilizing cell shape and microtubules at the cell cortex. We previously observed that Moesin localizes to the mitotic spindle; hence, we tested for the biological significance of this surprising localization and investigated whether it plays a direct role in spindle function. To separate the cortical and spindle functions of Moesin during mitosis we combined cell biological and genetic methods. We used early Drosophila embryos, in which mitosis occurs in the absence of a cell cortex, and found in vivo evidence for the direct requirement of Moesin in mitotic spindle assembly and function. We also found that the accumulation of Moesin precedes the construction of the microtubule spindle, and the fusiform structure formed by Moesin persists even after the microtubules have disassembled.
authors.affiliation: Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Temesvári krt. 62., Hungary.
authors.forename: Péter
authors.initials: P
authors.lastname: Vilmos
authors.affiliation: Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Temesvári krt. 62., Hungary.
authors.forename: Ildikó
authors.initials: I
authors.lastname: Kristó
authors.affiliation: Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Temesvári krt. 62., Hungary.
authors.forename: Szilárd
authors.initials: S
authors.lastname: Szikora
authors.affiliation: Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Temesvári krt. 62., Hungary.
authors.forename: Ferenc
authors.initials: F
authors.lastname: Jankovics
authors.affiliation: Department of Developmental and Cell Biology, University of California Irvine, Irvine, CA, 92697, USA.
authors.forename: Tamás
authors.initials: T
authors.lastname: Lukácsovich
authors.affiliation: Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Temesvári krt. 62., Hungary.
authors.forename: Beáta
authors.initials: B
authors.lastname: Kari
authors.affiliation: Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Temesvári krt. 62., Hungary.
authors.forename: Miklós
authors.initials: M
authors.lastname: Erdélyi
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D002453:Cell Cycle / Q000502:physiology; D048430:Cell Shape / Q000502:physiology; D003593:Cytoplasm / Q000378:metabolism; D004331:Drosophila melanogaster; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D008938:Mitosis / Q000502:physiology; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism*
chemical_list: D000199:Actins; D008565:Membrane Proteins; C099886:moesin, Drosophila; D017346:Protein Serine-Threonine Kinases
keywords: Drosophila; ERM; Moesin; actin; mitosis; spindle