Open Close
Solinet, S., Mahmud, K., Stewman, S.F., Ben El Kadhi, K., Decelle, B., Talje, L., Ma, A., Kwok, B.H., Carreno, S. (2013). The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex.  J. Cell Biol. 202(2): 251--260.
FlyBase ID
Publication Type
Research paper
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.
PubMed ID
PubMed Central ID
PMC3718980 (PMC) (EuropePMC)
Associated Information
Associated Files
Other Information
Secondary IDs
    Language of Publication
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    J. Cell Biol.
    Journal of Cell Biology
    Publication Year
    Data From Reference
    Genes (1)