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The actin‐binding ERM protein Moesin directly regulates spindle assembly and function during mitosis
Author(s) -
Vilmos Péter,
Kristó Ildikó,
Szikora Szilárd,
Jankovics Ferenc,
Lukácsovich Tamás,
Kari Beáta,
Erdélyi Miklós
Publication year - 2016
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.10607
Subject(s) - moesin , radixin , microbiology and biotechnology , mitosis , spindle apparatus , ezrin , microtubule , cell cortex , cytoskeleton , biology , spindle pole body , filamin , chemistry , cell division , cell , biochemistry
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.