Molecular requirements for the inter-subunit interaction and kinetochore recruitment of SKAP and Astrin

Alexandra Friese, Alex C. Faesen, Pim J. Huis in ‘t Veld, Josef Fischböck, Daniel Prumbaum, Arsen Petrovic, Stefan Raunser, Franz Herzog and Andrea Musacchio ()
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Alexandra Friese: Max Planck Institute of Molecular Physiology
Alex C. Faesen: Max Planck Institute of Molecular Physiology
Pim J. Huis in ‘t Veld: Max Planck Institute of Molecular Physiology
Josef Fischböck: Gene Center Munich, Ludwig-Maximilians-Universität München
Daniel Prumbaum: Max Planck Institute of Molecular Physiology
Arsen Petrovic: Max Planck Institute of Molecular Physiology
Stefan Raunser: Max Planck Institute of Molecular Physiology
Franz Herzog: Gene Center Munich, Ludwig-Maximilians-Universität München
Andrea Musacchio: Max Planck Institute of Molecular Physiology

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract Accurate chromosome segregation during cell division is crucial for propagating life and protects from cellular transformation. The SKAP:Astrin heterodimer localizes to spindle microtubules and to mature microtubule–kinetochore attachments during mitosis. Depletion of either subunit disrupts spindle structure and destabilizes kinetochore–microtubule attachments. Here, we identify molecular requirements for the inter-subunit interaction of SKAP and Astrin, and discuss requirements for their kinetochore recruitment. We also identify and characterize a microtubule-binding domain in SKAP, distinct from the SXIP motif that mediates end binding (EB) protein binding and plus end tracking, and show that it stimulates the growth-rate of microtubules, possibly through a direct interaction with tubulin. Mutations targeting this microtubule-binding domain impair microtubule plus-end tracking but not kinetochore targeting, and recapitulate many effects observed during depletion of SKAP. Collectively, our studies represent the first thorough mechanistic analysis of SKAP and Astrin, and significantly advance our functional understanding of these important mitotic proteins.

Date: 2016
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DOI: 10.1038/ncomms11407

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