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Cited by 56Microtubule and mitosis dynamicsProtein Structure and DynamicsATP Synthase and ATPases Research

Equilibrium studies of kinesin-nucleotide intermediates

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Rosenfeld, Steven S., Rener, Brenda, Correia, John J., Mayo, Matthew S., Cheung, Herbert C.·1996·Journal of Biological Chemistry
DOI 10.1074/jbc.271.16.9473
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Abstract

We have examined the energetics of the interactions of two kinesin constructs with nucleotide and microtubules to develop a structural model of kinesin-dependent motility. Dimerization of the constructs was found to reduce the maximum rate of the microtubule-activated kinesin ATPase 5-fold. Beryllium fluoride and aluminum fluoride also reduce this rate, and they increase the affinity of kinesin for microtubules. By contrast, inorganic phosphate reduces the affinity of a dimeric kinesin construct for microtubules. These findings are consistent with a model in which the kinesin head can assume one of two conformations, "strong" or "weak" binding, determined by the nature of the nucleotide that occupies the active site. Data for dimeric kinesin are consistent with a model in which kinesin.ATP binds to the microtubule in a strong state with positive cooperativity; hydrolysis of ATP to ADP+P(i) leads to dissociation of one of the attached heads and converts the second, attached head to a weak state; and dissociation of phosphate allows the second head to reattach. These results also argue that a large free energy change is associated with formation of kinesin.ADP.P(i) and that this step is the major pathway for dissociation of kinesin from the microtubule.

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  • The apparent MT binding constant of HK420 in COS lysates agrees with the apparent binding constant for MTs based on activation of the ATPase activity of purified dimeric kinesin constructs.

    “This value agrees with the apparent binding constant for MTs based on activation of the ATPase activity of purified dimeric kinesin constructs (Hackney, 1994, 1995; Rosenfeld et al., 1996; Jiang et al., 1997).”

    From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Rosenfeld et al., 1996

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Authors
Rosenfeld, S. S., Rener, B., Correia, J. J., Mayo, M. S., & Cheung, H. C.
Affiliations
  • University of Alabama at Birmingham (US)
  • University of Mississippi Medical Center (US)
Corresponding author
Rosenfeld, Steven S.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-04
Volume
271
Issue
16
Pages
9473-9482
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.271.16.9473
OpenAlex
W2093593955
Cited by
56
References
51
Citations by year
2026: 1 · 2025: 1 · 2020: 2 · 2019: 1 · 2017: 1 · 2016: 1 · 2014: 2 · 2013: 1 · 2012: 3
FWCI
2.10
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01ar031239-07, 5k08ns001500-03, 5p20ns031096-03)
  • National Institute of Neurological Disorders and Stroke (NS01500, NS31096)
  • National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR 31239)
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
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
kinesin, nucleotide binding, beryllium fluoride, aluminum fluoride, inorganic phosphate, cooperativity, ATP hydrolysis, kinesin motility, free energy
MeSH terms
Adenosine Diphosphate, Adenosine Triphosphatases, Adenosine Triphosphate, Adenylyl Imidodiphosphate, Base Sequence, Cloning, Molecular, Escherichia coli, Humans, Kinetics, Mathematics, Microtubules, Models, Structural, Models, Theoretical, Molecular Sequence Data, Phosphates, Protein Binding, Recombinant Proteins, Tubulin, Kinesins, DNA Primers

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