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DHTP is an allosteric inhibitor of the kinesin‐13 family of microtubule depolymerases
Author(s) -
Talje Lama,
Ben El Kadhi Khaled,
Atchia Kaleem,
Tremblay-Boudreault Thierry,
Carreno Sébastien,
Kwok Benjamin H.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.05.024
Subject(s) - kinesin , allosteric regulation , microtubule , microbiology and biotechnology , mitosis , microtubule polymerization , spindle apparatus , chemistry , biology , cell division , cell , tubulin , biochemistry , receptor
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.