| Autor: |
Solinet S; Cellular Mechanisms of Morphogenesis during Mitosis and Cell Motility, Université de Montréal, Montréal, Québec H3C 3J7, Canada., Mahmud K, Stewman SF, Ben El Kadhi K, Decelle B, Talje L, Ma A, Kwok BH, Carreno S |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of cell biology [J Cell Biol] 2013 Jul 22; Vol. 202 (2), pp. 251-60. Date of Electronic Publication: 2013 Jul 15. |
| DOI: |
10.1083/jcb.201304052 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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