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Cited by 73Microtubule and mitosis dynamicsProtein Structure and DynamicsForce Microscopy Techniques and Applications

KIF1D is a fast non‐processive kinesin that demonstrates novel K‐loop‐dependent mechanochemistry

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Rogers, Kevin R., Weiss, Stefan, Crevel, Isabelle, Brophy, Peter J., Geeves, Michael, Cross, Robert·2001·The EMBO Journal
DOI 10.1093/emboj/20.18.5101PMC PMC125638
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Abstract

The KIF1 subfamily members are monomeric and contain a number of amino acid inserts in surface loops. A particularly striking insertion of several lysine/arginine residues occurs in L12 and is called the K-loop. Two recent studies have employed both kinetic and single-molecule methods to investigate KIF1 motor properties and have produced very different conclusions about how these motors generate motility. Here we show that a hitherto unstudied member of this group, KIF1D, is not chemically processive and drives fast motility despite demonstrating a slow ATPase. The K-loop of KIF1D was analysed by deletion and insertion mutagenesis coupled with characterization by steady state and transient kinetics. Together, the results indicate that the K-loop not only increases the affinity of the motor for the MT, but crucially also inhibits its subsequent isomerization from weak to strong binding, with coupled ADP release. By stabilizing the weak binding, the K-loop establishes a pool of motors primed to undergo their power stroke.

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  • Each motor in groups acts as a tether to the MT and reduces unproductive diffusion along the MT.

    “The result implies that each motor in groups acts as a tether to the MT and reduces the unproductive diffusion along the MT, as discussed previously (36,45).”

    From Diffusion and Directed Movement (2008) · cites this paper as [45]

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Research works printed but not linked: 3

  1. Bloom G.S. (2001) The unc104/KIF1 family of kinesins. Curr. Opin. Cell Biol., 13, 36–40. [DOI] [PubMed] [Google Scholar]
  2. Cross R.A. (1999) Walking talking heads. Curr. Biol., 9, R854–R856. [DOI] [PubMed] [Google Scholar]
  3. Rogers K.R., Griffin,M. and Brophy,P.J. (1998) The secretory epithelial cells of the choroid plexus employ a novel kinesin-related protein. Brain Res. Mol. Brain Res., 55, 355. [DOI] [PubMed] [Google Scholar]

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Related

Authors
Rogers, K. R., Weiss, S., Crevel, I., Brophy, P. J., Geeves, M., & Cross, R.
Affiliations
  • Marie Curie (GB)
  • University of Kent (GB)
  • University of Edinburgh (GB)
Corresponding author
Cross, Robert
ORCID
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
2001-09-17
Volume
20
Issue
18
Pages
5101-5113
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
DOI
10.1093/emboj/20.18.5101
PMC
PMC125638
OpenAlex
W2002226865
Cited by
73
References
48
Citations by year
2024: 1 · 2023: 1 · 2022: 5 · 2021: 4 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 2 · 2012: 4
FWCI
2.15
Type
journal article
Language
en
Open access
Licence
Locations
  • The EMBO Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Kent Academic Repository (University of Kent) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
Keywords
K-loops, mechanochemistry, microtubule binding, ATPase kinetics, ADP release, power stroke, microtubule motor proteins, single-molecule motility
MeSH terms
Adenosine Diphosphate, Amino Acid Sequence, Animals, Biomechanical Phenomena, Kinetics, Microtubules, Models, Biological, Molecular Sequence Data, Movement, Nerve Tissue Proteins, Mutagenesis, Insertional, Kinesins, Sequence Deletion, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Molecular Motor Proteins, Amino Acid Motifs, ortho-Aminobenzoates

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