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Modulation of kinesin binding by the C-termini of tubulin
Modulation of kinesin binding by the C-termini of tubulin.
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The flexible tubulin C-terminal tails (CTTs) have recently been implicated in the walking mechanism of dynein and kinesin. To address their role in the case of conventional kinesin, we examined the structure of kinesin-microtubule (MT) complexes before and after CTT cleavage by subtilisin. Our results show that the CTTs directly modulate the motor-tubulin interface and the binding properties of motors. CTT cleavage increases motor binding stability, and kinesin appears to adopt a binding conformation close to the nucleotide-free configuration under most nucleotide conditions. Moreover, C-terminal cleavage results in trapping a transient motor-ADP-MT intermediate. Using SH3-tagged dimeric and monomeric constructs, we could also show that the position of the kinesin neck is not affected by the C-terminal segments of tubulin. Overall, our study reveals that the tubulin C-termini define the stability of the MT-kinesin complex in a nucleotide-dependent manner, and highlights the involvement of tubulin in the regulation of weak and strong kinesin binding states.
Skiniotis G, Cochran JC, Müller J, Mandelkow E, Gilbert SP, Hoenger A
The EMBO journal
2004-03-10 00:00
23
5
989-99
Adenosine Diphosphate,Adenylyl Imidodiphosphate,Animals,Cattle,Dimerization,Kinesin,Kinetics,Microtubules,Models, Molecular,Pliability,Protein Binding,Protein Structure, Tertiary,Tubulin,Tubulin,Adenylyl Imidodiphosphate,Adenosine Diphosphate,Kinesin
European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, Germany
EMBO J.
NIAMS K02 AR047841-02, NIGMS R01 GM054141-08
0261-4189
10.1038/sj.emboj.7600118
7600118
563
True
14976555
