ArticleBiophysical journal2006
Flexibility of the neck domain enhances Kinesin-1 motility under load.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- The Impact of Rate Formulations on Stochastic Molecular Motor Dynamics.Scientific reports · 2019Article
- Structural Correlation of the Neck Coil with the Coiled-coil (CC1)-Forkhead-associated (FHA) Tandem for Active Kinesin-3 KIF13A.The Journal of biological chemistry · 2016Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Biochemical and molecular dynamic simulation analysis of a weak coiled coil association between kinesin-II stalks.PloS one · 2012Article
- The Aspergillus nidulans CENP-E kinesin KipA is able to dimerize and to move processively along microtubules.Current genetics · 2011Article
- Extensibility of the extended tail domain of processive and nonprocessive myosin V molecules.Biophysical journal · 2009Article
- Mechanical design of translocating motor proteins.Cell biochemistry and biophysics · 2009Review
- Dissection of kinesin's processivity.PloS one · 2009Article
- Secondary structure and compliance of a predicted flexible domain in kinesin-1 necessary for cooperation of motors.Biophysical journal · 2008Article
- Cargo transport: molecular motors navigate a complex cytoskeleton.Current opinion in cell biology · 2008Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-1 is a dimeric motor protein that moves stepwise along microtubules. A two-stranded alpha-helical coiled-coil formed by the neck domain links the two heads of the molecule, and forces the motor heads to alternate. By exchanging the particularly soft neck region of the conventional kinesin from the fungus Neurospora crassa with an artificial, highly stable coiled-coil we investigated how this domain affects motor kinetics and motility. Under unloaded standard conditions, both motor constructs developed the same gliding velocity. However, in a force-feedback laser trap the mutant showed increasing motility defects with increasing loads, and did not reach wild-type velocities and run lengths. The stall force dropped significantly from 4.1 to 3.0 pN. These results indicate the compliance of kinesin's neck is important to sustain motility under load, and reveal a so far unknown constrain on the imperfect coiled-coil heptad pattern of Kinesin-1. We conclude that coiled-coil structures, a motif encountered in various types of molecular motors, are not merely a clamp for linking two heavy chains to a functional unit but may have specifically evolved to allow motor progression in a viscous, inhomogeneous environment or when several motors attached to a transported vesicle are required to cooperate efficiently.
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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.