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Cited by 63Microtubule and mitosis dynamicsProtein Structure and DynamicsEnzyme Structure and Function

The molecular structure of adrenal medulla kinesin

Hisanaga, Shin‐ichi, Murofushi, Hiromu, Okuhara, Koji, Sato, Reiko, Masuda, Yayoi, Sakai, Hikoichi, Hirokawa, Nobutaka·1989·Cell Motility
DOI 10.1002/cm.970120407
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Abstract

The molecular structure of bovine adrenal kinesin was studied by electron microscopy using the low-angle rotary shadowing technique. Adrenal kinesin exhibited either a folded or an extended configuration; the ratio of the two is dependent on the salt concentration. Almost all adrenal kinesin molecules were folded in a low-ionic solution, and the ratio of extended molecules increased to 40-50% in a solution containing 1 M ammonium acetate. Kinesin in the extended configuration displayed a rod-shaped structure with a mean length of about 80 nm. The morphologies of the ends were different; one end was composed of two globular particles, similar to the two-headed structure of myosin, while the other end had a more ill-defined structure, appearing either as a globular particle, an aggregate of two to four small granules, or a frayed, fan-like structure. The folded kinesin molecule possessed a hinge region in the middle of the rod, at about 32 nm from the neck of the two heads. In our preparations, the majority of adrenal kinesin molecules were folded at physiological salt concentrations. Adrenal kinesin bound to microtubules in the presence of adenylyl imidodiphosphate (AMP-PNP) also displayed a folded morphology.

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Crossref · 10.1002/cm.970120407

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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 Hisanaga 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 Hisanaga et al., 1989

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Authors
Hisanaga, S., Murofushi, H., Okuhara, K., Sato, R., Masuda, Y., Sakai, H., & Hirokawa, N.
Affiliations
The University of Tokyo (JP)
Corresponding author
Hisanaga, Shin‐ichi
ORCID
Venue
Cell Motility
Publisher
Wiley
Published
1989-01
Volume
12
Issue
4
Pages
264-272
ISSN
0886-1544 (ISSN-L)
DOI
10.1002/cm.970120407
OpenAlex
W2072888047
Cited by
63
References
40
Citations by year
2026: 2 · 2025: 3 · 2024: 1 · 2022: 3 · 2018: 1 · 2015: 1 · 2013: 1 · 2012: 2
FWCI
2.90
Type
journal article
Language
en
Open access
closed
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 5878 d)
Locations
  • Cell Motility and the Cytoskeleton (publishedVersion)
  • PubMed (publishedVersion)
Funders
Muscular Dystrophy Association
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 › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
protein conformation, salt concentration dependence, hinge region, microtubule binding, AMP-PNP, rotary shadowing, bovine adrenal medulla
MeSH terms
Acetates, Adrenal Medulla, Animals, Cattle, Electrophoresis, Polyacrylamide Gel, Microscopy, Electron, Microtubules, Nerve Tissue Proteins, Protein Conformation, Sodium Chloride, Kinesins

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