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Cited by 271Microtubule and mitosis dynamicsCancer-related Molecular PathwaysCancer Treatment and Pharmacology

Mutations in the kinesin-like protein Eg5 disrupting localization to the mitotic spindle

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Sawin, K E, Mitchison, T J·1995·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.92.10.4289PMC PMC41929
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Abstract

Eg5, a member of the bimC subfamily of kinesin-like microtubule motor proteins, localizes to spindle microtubules in mitosis but not to interphase microtubules. We investigated the molecular basis for spindle localization by transient transfection of Xenopus A6 cells with myc-tagged derivatives of Eg5. Expressed at constitutively high levels from a cytomegalovirus promoter, mycEg5 protein is cytoplasmic throughout interphase, begins to bind microtubules in early prophase, and remains localized to spindle and/or midbody microtubules through mitosis to the end of telophase. Both N- and C-terminal regions of Eg5 are required for this cell-cycle-regulated targeting. Eg5 also contains within its C-terminal domain a sequence conserved among bimC subfamily proteins that includes a potential p34cdc2 phosphorylation site. We show that mutation of a single threonine (T937) within this site to nonphosphorylatable alanine abolishes localization of the mutant protein to the spindle, whereas mutation of T937 to serine preserves spindle localization. We hypothesize that phosphorylation of Eg5 may regulate its localization to the spindle in the cell cycle.

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  • Phosphorylation by Cdk1 of the Eg5 tail is required for localization of Eg5 to the spindle microtubules.

    “The first example of this phosphoregulatory control was shown for the Kinesin-5s, where phosphorylation by Cdk1 of the Eg5 tail was shown to be required for localization of Eg5 to the spindle microtubules [25, 26].”

    From Regulatory mechanisms that control mitotic kinesins (2015) · cites this paper as [26]

    The Results show that replacing the C-terminal residue T937 with alanine abolishes Eg5 spindle localization, while replacing it with serine does not. The authors propose phosphorylation as an explanation but explicitly say they do not yet know whether Eg5 is phosphorylated in vivo; they do not establish that Cdk1 phosphorylation is required. (LLM, conf=0.90)

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Research works printed but not linked: 3

  1. Hoyt, M. A., He, L., Loo, K. K. & Saunders, W. S. (1992) J. Cell Biol. 118, 109-120.
  2. Erlich, H. A. (Stock- ton, New York), pp. 61-70.
  3. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Lab. Press, Plainview, NY), 2nd Ed.

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Authors
Sawin, K. E., & Mitchison, T. J.
Affiliations
University of California, San Francisco (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1995-05-09
Volume
92
Issue
10
Pages
4289-4293
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.92.10.4289
PMC
PMC41929
OpenAlex
W1977666960
Cited by
271
References
38
Citations by year
2026: 3 · 2025: 6 · 2024: 7 · 2023: 6 · 2022: 4 · 2021: 4 · 2020: 5 · 2019: 1 · 2018: 14 · 2017: 8 · 2016: 7 · 2015: 8 · 2014: 4 · 2013: 10 · 2012: 10
FWCI
3.78
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
Funders
  • National Institutes of Health (GM39565)
  • Directorate for Biological Sciences
  • National Institute of General Medical Sciences (R01-GM39565, R01GM039565)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
  • Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
Keywords
Eg5, microtubule binding, cell cycle regulation, threonine phosphorylation, C-terminal domain, mitosis
MeSH terms
Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cytomegalovirus, Microtubule-Associated Proteins, Spindle Apparatus, Molecular Sequence Data, Promoter Regions, Genetic, Recombinant Proteins, Transfection, Xenopus, Polymerase Chain Reaction, Mutagenesis, Site-Directed, Kinesins, Conserved Sequence, DNA Primers, Xenopus Proteins

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