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DHTP is an allosteric inhibitor of the kinesin-13 family of microtubule depolymerases.

Talje L, Ben El Kadhi K, Atchia K, Tremblay-Boudreault T, Carreno S, Kwok BH

Chemical Biology of Cell Division Laboratory, Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, P.O. Box 6128, Station Centre-Ville, Montréal, Québec H3C 3J7, Canada.

The kinesin-13 family of microtubule depolymerases is a major regulator of microtubule dynamics. RNA interference-induced knockdown studies have highlighted their importance in many cell division processes including spindle assembly and chromosome segregation. Since microtubule turnovers and most mitotic events are relatively rapid (in minutes or seconds), developing tools that offer faster control over protein functions is therefore essential to more effectively interrogate kinesin-13 activities in living cells. Here, we report the identification and characterization of a selective allosteric kinesin-13 inhibitor, DHTP. Using high resolution microscopy, we show that DHTP is cell permeable and can modulate microtubule dynamics in cells.

FEBS Lett. 2014;588(14):2315-20.

Pubmed ID: 24859087

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