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Cited by 477Microtubule and mitosis dynamicsGenetic and Kidney Cyst DiseasesProtein Structure and Dynamics

Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration

Hirokawa, Nobutaka, Pfister, K.Kevin, Yorifuji, Hiroshi, Wagner, Mark C., Brady, Scott T., Bloom, George S.·1989·Cell
DOI 10.1016/0092-8674(89)90691-0
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Abstract

Kinesin is a microtubule-activated ATPase thought to transport membrane-bounded organelles along MTs. To illuminate the structural basis for this function, EM was used to locate submolecular domains on bovine brain kinesin. Rotary shadowed kinesin appeared rod-shaped and approximately 80 nm long. One end of each molecule contained a pair of approximately 10 x 9 nm globular domains, while the opposite end was fan-shaped. Monoclonal antibodies against the approximately 124 kd heavy chains of kinesin decorated the globular structures, while those specific for the approximately 64 kd light chains labeled the fan-shaped end. Quick-freeze, deep-etch EM was used to analyze MTs polymerized from tubulin and cross-linked to latex microspheres by kinesin. Microspheres frequently attached to MTs by arm-like structures, 25-30 nm long. The MT attachment sites often appeared as one or two approximately 10 nm globular bulges. Morphologically similar cross-links were observed by quick-freeze, deep-etch EM between organelles and MTs in the neuronal cytoskeleton in vivo. These collective observations suggest that bovine brain kinesin binds to MTs by globular domains that contain the heavy chains, and that the attachment sites for organelles are at the opposite, fan-shaped end of kinesin, where the light chains are located.

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Crossref · 10.1016/0092-8674(89)90691-0

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56 of 56 references verified0 citation errors · 0 not checkable

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  • At physiological salt concentrations, purified kinesin is in a folded conformation in which the tail comes close to the motor domain, while in high salt, kinesin is in an extended conformation.

    “At physiological salt concentrations, purified kinesin is in a folded conformation in which the tail comes close to the motor domain, while, in high salt, kinesin is in an extended conformation.”

    From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hirokawa et al., 1989

  • The sedimentation coefficient of 9S determined for kinesin in cell lysates corresponds to the folded conformation of purified kinesin as determined by sedimentation and electron microscopy analysis.

    “Indeed, the sedimentation coefficient of 9S determined for kinesin in cell lysates corresponds to the folded conformation of purified kinesin as determined by sedimentation and electron microscopy analysis (Hirokawa et al., 1989; Hisanaga et al., 1989; Hackney et al., 1992).”

    From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hirokawa et al., 1989

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Authors
Hirokawa, N., Pfister, K. K., Yorifuji, H., Wagner, M. C., Brady, S. T., & Bloom, G. S.
Affiliations
  • The University of Tokyo (JP)
  • The University of Texas Southwestern Medical Center (US)
ORCID
Venue
Cell
Publisher
Elsevier BV
Published
1989-03
Volume
56
Issue
5
Pages
867-878
ISSN
0092-8674 (ISSN-L)
DOI
10.1016/0092-8674(89)90691-0
OpenAlex
W2004290556
Cited by
477
References
56
Citations by year
2026: 5 · 2025: 12 · 2024: 7 · 2023: 12 · 2022: 8 · 2021: 14 · 2020: 7 · 2019: 4 · 2018: 14 · 2017: 7 · 2016: 12 · 2015: 9 · 2014: 8 · 2013: 12 · 2012: 11
FWCI
13.16
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Cell (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation
  • National Institutes of Health (DMB-8701164, GM10143, NS23888)
  • Welch Foundation (l-1077)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
kinesin, microtubule binding, heavy chain, light chain, organelle transport, rotary shadowing, microtubule assembly, latex microspheres, neuronal cytoskeleton, bovine brain
MeSH terms
Adenosine Triphosphatases, Animals, Antibodies, Monoclonal, Binding Sites, Brain, Cattle, Freeze Etching, Microscopy, Electron, Microtubules, Molecular Weight, Nerve Tissue Proteins, Spinal Cord, Blotting, Western, Kinesins

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