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Microtubule minus-end aster organization is driven by processive HSET-tubulin clusters

Author

Listed:
  • Stephen R. Norris

    (Vanderbilt University
    Vanderbilt University Medical Center)

  • Seungyeon Jung

    (Vanderbilt University)

  • Prashant Singh

    (Vanderbilt University)

  • Claire E. Strothman

    (Vanderbilt University)

  • Amanda L. Erwin

    (Vanderbilt University
    University of Michigan Medical School
    University of Michigan Medical School)

  • Melanie D. Ohi

    (Vanderbilt University
    University of Michigan Medical School
    University of Michigan Medical School)

  • Marija Zanic

    (Vanderbilt University
    Vanderbilt University)

  • Ryoma Ohi

    (Vanderbilt University
    University of Michigan Medical School
    University of Michigan Medical School)

Abstract

Higher-order structures of the microtubule (MT) cytoskeleton are comprised of two architectures: bundles and asters. Although both architectures are critical for cellular function, the molecular pathways that drive aster formation are poorly understood. Here, we study aster formation by human minus-end-directed kinesin-14 (HSET/KIFC1). We show that HSET is incapable of forming asters from preformed, nongrowing MTs, but rapidly forms MT asters in the presence of soluble (non-MT) tubulin. HSET binds soluble (non-MT) tubulin via its N-terminal tail domain to form heterogeneous HSET-tubulin clusters containing multiple motors. Cluster formation induces motor processivity and rescues the formation of asters from nongrowing MTs. We then show that excess soluble (non-MT) tubulin stimulates aster formation in HeLa cells overexpressing HSET during mitosis. We propose a model where HSET can toggle between MT bundle and aster formation in a manner governed by the availability of soluble (non-MT) tubulin.

Suggested Citation

  • Stephen R. Norris & Seungyeon Jung & Prashant Singh & Claire E. Strothman & Amanda L. Erwin & Melanie D. Ohi & Marija Zanic & Ryoma Ohi, 2018. "Microtubule minus-end aster organization is driven by processive HSET-tubulin clusters," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04991-2
    DOI: 10.1038/s41467-018-04991-2
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    Cited by:

    1. Xinglei Liu & Lu Rao & Weihong Qiu & Florian Berger & Arne Gennerich, 2024. "Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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