ArticleBiophysical journal2015
Kinesin-2 KIF3AC and KIF3AB Can Drive Long-Range Transport along Microtubules.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- Heterotrimeric kinesin-2 autoinhibition mediated by interactions of the CC2 and proximal tail domains with the motor domains is essential for cilium formation and maintenance.bioRxiv : the preprint server for biology · 2026Article
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- The two-step cargo recognition mechanism of heterotrimeric kinesin.EMBO reports · 2023Article
- KAP is the neuronal organelle adaptor for Kinesin-2 KIF3AB and KIF3AC.Molecular biology of the cell · 2022Article
- Tau differentially regulates the transport of early endosomes and lysosomes.Molecular biology of the cell · 2022Article
- The mechanochemistry of the kinesin-2 KIF3AC heterodimer is related to strain-dependent kinetic properties of KIF3A and KIF3C.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Suppression of KIF3A inhibits triple negative breast cancer growth and metastasis by repressing Rb-E2F signaling and epithelial-mesenchymal transition.Cancer science · 2020Article
- Molecular Motor KIF3B Acts as a Key Regulator of Dendritic Architecture in Cortical Neurons.Frontiers in cellular neuroscience · 2020Article
- The ability of the kinesin-2 heterodimer KIF3AC to navigate microtubule networks is provided by the KIF3A motor domain.The Journal of biological chemistry · 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
- Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018Review
- Kinesin-2 motors adapt their stepping behavior for processive transport on axonemes and microtubules.EMBO reports · 2017Article
- Homodimeric Kinesin-2 KIF3CC Promotes Microtubule Dynamics.Biophysical journal · 2017Article
- Intraflagellar transport: mechanisms of motor action, cooperation, and cargo delivery.The FEBS journal · 2017Review
- Intraflagellar transport velocity is governed by the number of active KIF17 and KIF3AB motors and their motility properties under load.Proceedings of the National Academy of Sciences of the United States of America · 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
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Mammalian KIF3AC is classified as a heterotrimeric kinesin-2 that is best known for organelle transport in neurons, yet in vitro studies to characterize its single molecule behavior are lacking. The results presented show that a KIF3AC motor that includes the native helix α7 sequence for coiled-coil formation is highly processive with run lengths of ∼1.23 μm and matching those exhibited by conventional kinesin-1. This result was unexpected because KIF3AC exhibits the canonical kinesin-2 neck-linker sequence that has been reported to be responsible for shorter run lengths observed for another heterotrimeric kinesin-2, KIF3AB. However, KIF3AB with its native neck linker and helix α7 is also highly processive with run lengths of ∼1.62 μm and exceeding those of KIF3AC and kinesin-1. Loop L11, a component of the microtubule-motor interface and implicated in activating ADP release upon microtubule collision, is significantly extended in KIF3C as compared with other kinesins. A KIF3AC encoding a truncation in KIF3C loop L11 (KIF3ACΔL11) exhibited longer run lengths at ∼1.55 μm than wild-type KIF3AC and were more similar to KIF3AB run lengths, suggesting that L11 also contributes to tuning motor processivity. The steady-state ATPase results show that shortening L11 does not alter kcat, consistent with the observation that single molecule velocities are not affected by this truncation. However, shortening loop L11 of KIF3C significantly increases the microtubule affinity of KIF3ACΔL11, revealing another structural and mechanistic property that can modulate processivity. The results presented provide new, to our knowledge, insights to understand structure-function relationships governing processivity and a better understanding of the potential of KIF3AC for long-distance transport in neurons.
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Registered trials
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.