Article
- The EMBO Journal (2004) 23, 989 - 999
- doi:10.1038/sj.emboj.7600118
Published online: 19 February 2004
Subject Categories:
Modulation of kinesin binding by the C-termini of tubulin
Georgios Skiniotis1,a, Jared C Cochran2, Jens Müller3, Eckhard Mandelkow3, Susan P Gilbert2 and Andreas Hoenger1
- European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, Germany
- Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA
- Max Planck Unit for Structural Molecular Biology, DESY-Hamburg, Hamburg, Germany
Correspondence to:
Andreas Hoenger, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany. Tel.: +49 6221 387453; Fax: +49 6221 387519; E-mail: hoenger@embl-heidelberg.de
aPresent address: Harvard Medical School, Department of Cell Biology, 240 Longwood Avenue Boston, MA, 02115, USA
Received 26 November 2003; Accepted 14 January 2004
Abstract
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.
Keywords:
- cryo-electron microscopy,
- kinesin,
- kinesin neck-linker,
- SH3 domain,
- tubulin C-terminus
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