ArticleMolecular biology of the cell2005
The complex interplay between the neck and hinge domains in kinesin-1 dimerization and motor activity.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022Review
- MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules.The Journal of biological chemistry · 2019Article
- Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Traffic control: regulation of kinesin motors.Nature reviews. Molecular cell biology · 2009Review
- Structure of the complex of a mitotic kinesin with its calcium binding regulator.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The Kinesin-1 tail conformationally restricts the nucleotide pocket.Biophysical journal · 2009Article
- Dissection of kinesin's processivity.PloS one · 2009Article
- The kinesin-1 motor protein is regulated by a direct interaction of its head and tail.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Myosin V stepping mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells.The Journal of cell biology · 2007Article
- Two binding partners cooperate to activate the molecular motor Kinesin-1.The Journal of cell biology · 2007Article
- The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly.Molecular biology of the cell · 2007Article
- The distance that kinesin-1 holds its cargo from the microtubule surface measured by fluorescence interference contrast microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Autoinhibition regulates the motility of the C. elegans intraflagellar transport motor OSM-3.The Journal of cell biology · 2006Article
- Flexibility of the neck domain enhances Kinesin-1 motility under load.Biophysical journal · 2006Article
- Review: regulation mechanisms of Kinesin-1.Journal of muscle research and cell motility · 2006Review
- Back on track - on the role of the microtubule for kinesin motility and cellular function.Journal of muscle research and cell motility · 2006Review
- Interaction of kinesin motors, microtubules, and MAPs.Journal of muscle research and cell motility · 2006Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 non-coiled-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. On the basis of 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.