ArticleBiophysical journal2013
A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Dissecting the pH Sensitivity of Kinesin-Driven Transport.The journal of physical chemistry. B · 2024Article
- VASH1-SVBP and VASH2-SVBP generate different detyrosination profiles on microtubules.The Journal of cell biology · 2023Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity.Nature cell biology · 2020Article
- The disordered N-terminus of HDAC6 is a microtubule-binding domain critical for efficient tubulin deacetylation.The Journal of biological chemistry · 2020Article
- KIF15 nanomechanics and kinesin inhibitors, with implications for cancer chemotherapeutics.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Cooperative Accumulation of Dynein-Dynactin at Microtubule Minus-Ends Drives Microtubule Network Reorganization.Developmental cell · 2018Article
- The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.The Journal of biological chemistry · 2017Article
- Schizosaccharomyces pombe kinesin-5 switches direction using a steric blocking mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Kinesin-5 is a microtubule polymerase.Nature communications · 2015Article
- Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality.The Journal of biological chemistry · 2015Article
- Regulatory mechanisms that control mitotic kinesins.Experimental cell research · 2015Review
- Tau co-organizes dynamic microtubule and actin networks.Scientific reports · 2015Article
- Mechanism and regulation of kinesin-5, an essential motor for the mitotic spindle.Biology of the cell · 2014Review
- Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homotetrameric kinesin-5 motors are essential for chromosome separation and assembly of the mitotic spindle. These kinesins bind between two microtubules (MTs) and slide them apart, toward the spindle poles. This process must be tightly regulated in mitosis. In in vitro assays, Eg5 moves diffusively on single MTs and switches to a directed mode between MTs. How allosteric communication between opposing motor domains works remains unclear, but kinesin-5 tail domains may be involved. Here we present a single-molecule fluorescence study of a tetrameric kinesin-1 head/kinesin-5 tail chimera, DK4mer. This motor exhibited fast processive motility on single MTs interrupted by pauses. Like Eg5, DK4mer diffused along MTs with ADP, and slid antiparallel MTs apart with ATP. In contrast to Eg5, diffusive and processive periods were clearly distinguishable. This allowed us to measure transition rates among states and for unbinding as a function of buffer ionic strength. These data, together with results from controls using tail-less dimers, indicate that there are two modes of interaction with MTs, separated by an energy barrier. This result suggests a scheme of motor regulation that involves switching between two bound states, possibly allosterically controlled by the opposing tetramer end. Such a scheme is likely to be relevant for the regulation of native kinesin-5 motors.
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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.