ArticleBiophysical journal2005
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 57 citations in OpenAlex.
- Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.Biophysical journal · 2026Article
- Neck region-microtubule interactions direct counterclockwise stepping of kinesin-1.Biophysical journal · 2026Article
- Dissecting the pH Sensitivity of Kinesin-Driven Transport.The journal of physical chemistry. B · 2024Article
- Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin.International journal of molecular sciences · 2022Article
- Tracking the Amide I and αCOO- Terminal ν(C=O) Raman Bands in a Family of l-Glutamic Acid-Containing Peptide Fragments: A Raman and DFT Study.Molecules (Basel, Switzerland) · 2021Article
- Backstepping Mechanism of Kinesin-1.Biophysical journal · 2020Article
- Processivity vs. Beating: Comparing Cytoplasmic and Axonemal Dynein Microtubule Binding Domain Association with Microtubule.International journal of molecular sciences · 2019Article
- E-hooks provide guidance and a soft landing for the microtubule binding domain of dynein.Scientific reports · 2018Article
- Processive Kinesin-14 HSET Exhibits Directional Flexibility Depending on Motor Traffic.Current biology : CB · 2018Article
- Article
- Collective Force Regulation in Anti-parallel Microtubule Gliding by Dimeric Kif15 Kinesin Motors.Current biology : CB · 2017Article
- Kinesin Processivity Is Determined by a Kinetic Race from a Vulnerable One-Head-Bound State.Biophysical journal · 2017Article
- The motility of axonemal dynein is regulated by the tubulin code.Biophysical journal · 2014Article
- Regulation of microtubule motors by tubulin isotypes and post-translational modifications.Nature cell biology · 2014Article
- A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility.Biophysical journal · 2013Article
- A second tubulin binding site on the kinesin-13 motor head domain is important during mitosis.PloS one · 2013Article
- Structural insights into WHAMM-mediated cytoskeletal coordination during membrane remodeling.The Journal of cell biology · 2012Article
- The nucleotide-binding state of microtubules modulates kinesin processivity and the ability of Tau to inhibit kinesin-mediated transport.The Journal of biological chemistry · 2011Article
- A structural perspective on the dynamics of kinesin motors.Biophysical journal · 2011Article
- Electrostatically biased binding of kinesin to microtubules.PLoS biology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesins are dimeric motor proteins that move processively along microtubules. It has been proposed that the processivity of conventional kinesins is increased by electrostatic interactions between the positively charged neck of the motor and the negatively charged C-terminus of tubulin (E-hook). In this report we challenge this anchoring hypothesis by studying the motility of a fast fungal kinesin from Neurospora crassa (NcKin). NcKin is highly processive despite lacking the positive charges in the neck. We present a detailed analysis of how proteolytic removal of the E-hook affects truncated monomeric and dimeric constructs of NcKin. Upon digestion we observe a strong reduction of the processivity and speed of dimeric motor constructs. Monomeric motors with truncated or no neck display the same reduction of microtubule gliding speed as dimeric constructs, suggesting that the E-hook interacts with the head only. The E-hook has no effect on the strongly bound states of NcKin as microtubule digestion does not alter the stall forces produced by single dimeric motors, suggesting that the E-hook affects the interaction site of the kinesin.ADP-head and the microtubule. In fact, kinetic and binding experiments indicate that removal of the E-hook shifts the binding equilibrium of the weakly attached kinesin.ADP-head toward a more strongly bound state, which may explain reduced processivity and speed on digested microtubules.
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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.