ArticleProceedings of the National Academy of Sciences of the United States of America2002
Coordination of kinesin's two heads studied with mutant heterodimers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- How Cytoplasmic Dynein Couples ATP Hydrolysis Cycle to Diverse Stepping Motions: Kinetic Modeling.Biophysical journal · 2020Article
- Step Sizes and Rate Constants of Single-headed Cytoplasmic Dynein Measured with Optical Tweezers.Scientific reports · 2018Article
- Reversal of axonal growth defects in an extraocular fibrosis model by engineering the kinesin-microtubule interface.Nature communications · 2016Article
- Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013Review
- Article
- Electrostatically biased binding of kinesin to microtubules.PLoS biology · 2011Article
- The kinesin-13 MCAK has an unconventional ATPase cycle adapted for microtubule depolymerization.The EMBO journal · 2011Article
- Mechanism of processive movement of monomeric and dimeric kinesin molecules.International journal of biological sciences · 2010Review
- Interactions between subunits in heterodimeric Ncd molecules.The Journal of biological chemistry · 2009Article
- A mobile kinesin-head intermediate during the ATP-waiting state.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Processive movement by a kinesin heterodimer with an inactivating mutation in one head.Biochemistry · 2008Article
- Single-headed mode of kinesin-5.EMBO reports · 2008Article
- How kinesin waits between steps.Nature · 2007Article
- Two distinct modes of processive kinesin movement in mixtures of ATP and AMP-PNP.The Journal of general physiology · 2007Article
- High-resolution, single-molecule measurements of biomolecular motion.Annual review of biophysics and biomolecular structure · 2007Review
- Long-range cooperative binding of kinesin to a microtubule in the presence of ATP.The Journal of cell biology · 2005Article
- Article
- A mutant heterodimeric myosin with one inactive head generates maximal displacement.The Journal of cell biology · 2003Article
- Revealingly odd couples.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
A conventional kinesin molecule has two identical catalytic domains (heads) and is thought to use them alternately to move processively, with 8-nm steps. To clarify how each head contributes to the observed steps, we have constructed heterodimeric kinesins that consist of two distinct heads. The heterodimers in which one of the heads is mutated in a microtubule-binding loop moved processively, even when the parent mutant homodimers bound too weakly to retain microtubules in microtubule-gliding assays. The velocities of the heterodimers were only slightly higher than those of the mutant homodimers, although mixtures of these weak-binding mutant homodimers and the WT dimers moved microtubules at a velocity similar to the WT. Thus, the mutant head affects the motility of the WT head only when they are in the same molecule. The maximum force a single heterodimer produced in optical trapping nanometry was intermediate between the WT and mutant homodimers, indicating that both heads contribute to the maximum force at the same time. These results demonstrate close collaboration of kinesin's two heads in producing force and motility.
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