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MBC in Press, published online ahead of print May 18, 2005
Mol. Biol. Cell 10.1091/mbc.E04-11-0957

A more recent version of this article appeared on August 1, 2005
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Submitted on November 2, 2004
Revised on May 3, 2005
Accepted on May 11, 2005

The Complex Interplay between the Neck and Hinge Domains in Kinesin-1 Dimerization and Motor Activity

Friederike Bathe, Katrin Hahlen, Renate Dombi, Lucia Driller, Manfred Schliwa, and Guenther Woehlke

Department of Cell Biology, Adolf-Butenandt-Institute, University of Munich, D-80336 Munich, Germany

Monitoring Editor: J. Richard McIntosh

Kinesin-1 dimerizes via the coiled-coil neck domain. In contrast to animal kinesins, neck dimerization of the fungal kinesin-1 NcKin requires additional residues from the hinge. Using chimeric constructs containing or lacking fungal-specific elements, the proximal part of the hinge was shown to stabilize the neck coiled-coil conformation in a complex manner. The conserved fungal kinesin hinge residue W384 caused neck coiled-coil formation in a chimeric NcKin construct, including parts of the human kinesin-1 stalk. The stabilizing effect was retained in a NcKinW384F mutant, suggesting important {pi}-stacking interactions. Without the stalk, W384 was not sufficient to induce coiled-coil formation, indicating that W384 is part of a cluster of several residues required for neck coiled-coil folding. A W384-less chimera of NcKin and human kinesin possessed a noncoiled-coil neck conformation and showed inhibited activity that could be reactivated when artificial interstrand disulfide bonds were used to stabilize the neck coiled-coil conformation. Based on yeast two-hybrid data, we propose that the proximal hinge can bind kinesin’s cargo-free tail domain and causes inactivation of kinesin by disrupting the neck coiled-coil conformation.

Address correspondence to: Guenther Woehlke (guenther.woehlke{at}lrz.uni-muenchen.de)




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