ArticleThe Journal of biological chemistry2015
Processivity of the kinesin-2 KIF3A results from rear head gating and not front head gating.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak interhead coordination.Biophysical journal · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak inter-head coordination.bioRxiv : the preprint server for biology · 2025Article
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- KIF1A is kinetically tuned to be a superengaging motor under hindering loads.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Synergy between inhibitors of two mitotic spindle assembly motors undermines an adaptive response.Molecular biology of the cell · 2022Article
- Article
- A kinetic dissection of the fast and superprocessive kinesin-3 KIF1A reveals a predominant one-head-bound state during its chemomechanical cycle.The Journal of biological chemistry · 2020Article
- The Tail of Kinesin-14a in Giardia Is a Dual Regulator of Motility.Current biology : CB · 2020Article
- The crowding dynamics of the motor protein kinesin-II.PloS one · 2020Article
- Kinesin-5 Promotes Microtubule Nucleation and Assembly by Stabilizing a Lattice-Competent Conformation of Tubulin.Current biology : CB · 2019Article
- The Orphan Kinesin PAKRP2 Achieves Processive Motility via a Noncanonical Stepping Mechanism.Biophysical journal · 2019Article
- Motor Dynamics Underlying Cargo Transport by Pairs of Kinesin-1 and Kinesin-3 Motors.Biophysical journal · 2019Article
- Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors.Molecules (Basel, Switzerland) · 2019Article
- Kinesin-2 heterodimerization alters entry into a processive run along the microtubule but not stepping within the run.The Journal of biological chemistry · 2018Article
- Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018Review
- Motor Reattachment Kinetics Play a Dominant Role in Multimotor-Driven Cargo Transport.Biophysical journal · 2018Article
- High-Resolution Single-Molecule Kinesin Assays at kHz Frame Rates.Methods in molecular biology (Clifton, N.J.) · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The kinesin-2 family motor KIF3A/B works together with dynein to bidirectionally transport intraflagellar particles, melanosomes, and neuronal vesicles. Compared with kinesin-1, kinesin-2 is less processive, and its processivity is more sensitive to load, suggesting that processivity may be controlled by different gating mechanisms. We used stopped-flow and steady-state kinetics experiments, along with single-molecule and multimotor assays to characterize the entire kinetic cycle of a KIF3A homodimer that exhibits motility similar to that of full-length KIF3A/B. Upon first encounter with a microtubule, the motor rapidly exchanges both mADP and mATP. When adenosine 5'-[(β,γ)-imido]triphosphate was used to entrap the motor in a two-head-bound state, exchange kinetics were unchanged, indicating that rearward strain in the two-head-bound state does not alter nucleotide binding to the front head. A similar lack of front head gating was found when intramolecular strain was enhanced by shortening the neck linker domain from 17 to 14 residues. In single-molecule assays in ADP, the motor dissociates at 2.1 s(-1), 20-fold slower than the stepping rate, demonstrating the presence of rear head gating. In microtubule pelleting assays, the KD(Mt) is similar in ADP and ATP. The data and accompanying simulations suggest that, rather than KIF3A processivity resulting from strain-dependent regulation of nucleotide binding (front head gating), the motor spends a significant fraction of its hydrolysis cycle in a low affinity state but dissociates only slowly from this state. This work provides a mechanism to explain differences in the load-dependent properties of kinesin-1 and kinesin-2.
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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.