Paclitaxel induces NM2-dependent cellular contraction independent of microtubule acetylation in live cells
Asensio-Juarez, G.; Perez-Diaz, R.; Ramos-Solano, H.; Garrido-Casado, M.; Talayero, V. C.; Vicente-Manzanares, M.
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In this study, we have investigated the crosstalk between microtubule dynamics and actomyosin contractility in cancer cells treated with taxanes, which are chemotherapeutics agents used to treat solid tumors. We found that paclitaxel (PTXL) induced cell contraction through a mechanism that involves the rapid (<1min) dissociation of GEF-H1 from microtubules and phosphorylation and activation of NM2 in a RhoA-dependent manner. This effect is relatively independent of microtubule acetylation since inhibition of tubulin deacetylase HDAC6 did not mimic the effect of PTXL, promoting instead a slow release of GEF-H1 from microtubules and lagged accumulation of phosphorylated NM2. Unexpectedly, depletion of tubulin acetyl transferase TAT1 also induced NM2 phosphorylation, indicating that microtubule acetylation maintains contractile homeostasis. Together, these results indicate that PTXL induces rapid cellular contraction dependent on the GEF-H1-RhoA-ROCK axis, whereas microtubule acetylation maintains appropriate levels of cellular contractility by exerting long-term control on NM2 phosphorylation and actomyosin organization.
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