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Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality.

Publication ,  Journal Article
Düselder, A; Fridman, V; Thiede, C; Wiesbaum, A; Goldstein, A; Klopfenstein, DR; Zaitseva, O; Janson, ME; Gheber, L; Schmidt, CF
Published in: The Journal of biological chemistry
July 2015

The bipolar kinesin-5 motors are one of the major players that govern mitotic spindle dynamics. Their bipolar structure enables them to cross-link and slide apart antiparallel microtubules (MTs) emanating from the opposing spindle poles. The budding yeast kinesin-5 Cin8 was shown to switch from fast minus-end- to slow plus-end-directed motility upon binding between antiparallel MTs. This unexpected finding revealed a new dimension of cellular control of transport, the mechanism of which is unknown. Here we have examined the role of the C-terminal tail domain of Cin8 in regulating directionality. We first constructed a stable dimeric Cin8/kinesin-1 chimera (Cin8Kin), consisting of head and neck linker of Cin8 fused to the stalk of kinesin-1. As a single dimeric motor, Cin8Kin switched frequently between plus and minus directionality along single MTs, demonstrating that the Cin8 head domains are inherently bidirectional, but control over directionality was lost. We next examined the activity of a tetrameric Cin8 lacking only the tail domains (Cin8Δtail). In contrast to wild-type Cin8, the motility of single molecules of Cin8Δtail in high ionic strength was slow and bidirectional, with almost no directionality switches. Cin8Δtail showed only a weak ability to cross-link MTs in vitro. In vivo, Cin8Δtail exhibited bias toward the plus-end of the MTs and was unable to support viability of cells as the sole kinesin-5 motor. We conclude that the tail of Cin8 is not necessary for bidirectional processive motion, but is controlling the switch between plus- and minus-end-directed motility.

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Published In

The Journal of biological chemistry

DOI

EISSN

1083-351X

ISSN

0021-9258

Publication Date

July 2015

Volume

290

Issue

27

Start / End Page

16841 / 16850

Related Subject Headings

  • Sequence Deletion
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Protein Structure, Tertiary
  • Microtubules
  • Kinesins
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences
  • 32 Biomedical and clinical sciences
  • 31 Biological sciences
 

Citation

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Düselder, A., Fridman, V., Thiede, C., Wiesbaum, A., Goldstein, A., Klopfenstein, D. R., … Schmidt, C. F. (2015). Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality. The Journal of Biological Chemistry, 290(27), 16841–16850. https://doi.org/10.1074/jbc.m114.620799
Düselder, André, Vladimir Fridman, Christina Thiede, Alice Wiesbaum, Alina Goldstein, Dieter R. Klopfenstein, Olga Zaitseva, Marcel E. Janson, Larisa Gheber, and Christoph F. Schmidt. “Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality.The Journal of Biological Chemistry 290, no. 27 (July 2015): 16841–50. https://doi.org/10.1074/jbc.m114.620799.
Düselder A, Fridman V, Thiede C, Wiesbaum A, Goldstein A, Klopfenstein DR, et al. Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality. The Journal of biological chemistry. 2015 Jul;290(27):16841–50.
Düselder, André, et al. “Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality.The Journal of Biological Chemistry, vol. 290, no. 27, July 2015, pp. 16841–50. Epmc, doi:10.1074/jbc.m114.620799.
Düselder A, Fridman V, Thiede C, Wiesbaum A, Goldstein A, Klopfenstein DR, Zaitseva O, Janson ME, Gheber L, Schmidt CF. Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality. The Journal of biological chemistry. 2015 Jul;290(27):16841–16850.

Published In

The Journal of biological chemistry

DOI

EISSN

1083-351X

ISSN

0021-9258

Publication Date

July 2015

Volume

290

Issue

27

Start / End Page

16841 / 16850

Related Subject Headings

  • Sequence Deletion
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Protein Structure, Tertiary
  • Microtubules
  • Kinesins
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences
  • 32 Biomedical and clinical sciences
  • 31 Biological sciences