ArticleThe Journal of biological chemistry2014
Kinesin-2 KIF3AB exhibits novel ATPase characteristics.
Article in The Journal of biological chemistry, 2014. 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, 15 citations in OpenAlex.
- Pathogenic mutations in the kinesin-3 motor KIF1A diminish force generation and movement through allosteric mechanisms.The Journal of cell biology · 2021Article
- 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
- Interaction of heterotrimeric kinesin-II with IFT-B-connecting tetramer is crucial for ciliogenesis.The Journal of cell biology · 2018Article
- An allosteric propofol-binding site in kinesin disrupts kinesin-mediated processive movement on microtubules.The Journal of biological chemistry · 2018Article
- Altered chemomechanical coupling causes impaired motility of the kinesin-4 motors KIF27 and KIF7.The Journal of cell biology · 2018Article
- Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018Review
- Homodimeric Kinesin-2 KIF3CC Promotes Microtubule Dynamics.Biophysical journal · 2017Article
- Common general anesthetic propofol impairs kinesin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Heterodimerization of Kinesin-2 KIF3AB Modulates Entry into the Processive Run.The Journal of biological chemistry · 2016Article
- Family-specific Kinesin Structures Reveal Neck-linker Length Based on Initiation of the Coiled-coil.The Journal of biological chemistry · 2016Article
- Fast or Slow, Either Head Can Start the Processive Run of Kinesin-2 KIF3AC.The Journal of biological chemistry · 2016Article
- Kinesin-2 KIF3AC and KIF3AB Can Drive Long-Range Transport along Microtubules.Biophysical journal · 2015Article
- The Mechanochemical Cycle of Mammalian Kinesin-2 KIF3A/B under Load.Current biology : CB · 2015Article
- Processivity of the kinesin-2 KIF3A results from rear head gating and not front head gating.The Journal of biological chemistry · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
KIF3AB is an N-terminal processive kinesin-2 family member best known for its role in intraflagellar transport. There has been significant interest in KIF3AB in defining the key principles that underlie the processivity of KIF3AB in comparison with homodimeric processive kinesins. To define the ATPase mechanism and coordination of KIF3A and KIF3B stepping, a presteady-state kinetic analysis was pursued. For these studies, a truncated murine KIF3AB was generated. The results presented show that microtubule association was fast at 5.7 μm(-1) s(-1), followed by rate-limiting ADP release at 12.8 s(-1). ATP binding at 7.5 μm(-1) s(-1) was followed by an ATP-promoted isomerization at 84 s(-1) to form the intermediate poised for ATP hydrolysis, which then occurred at 33 s(-1). ATP hydrolysis was required for dissociation of the microtubule·KIF3AB complex, which was observed at 22 s(-1). The dissociation step showed an apparent affinity for ATP that was very weak (K½,ATP at 133 μm). Moreover, the linear fit of the initial ATP concentration dependence of the dissociation kinetics revealed an apparent second-order rate constant at 0.09 μm(-1) s(-1), which is inconsistent with fast ATP binding at 7.5 μm(-1) s(-1) and a Kd ,ATP at 6.1 μm. These results suggest that ATP binding per se cannot account for the apparent weak K½,ATP at 133 μm. The steady-state ATPase Km ,ATP, as well as the dissociation kinetics, reveal an unusual property of KIF3AB that is not yet well understood and also suggests that the mechanochemistry of KIF3AB is tuned somewhat differently from homodimeric processive kinesins.
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