Abad, M. A., Medina, B., Santamaria, A., Zou, J., Plasberg-Hill, C., Madhumalar, A., … Jeyaprakash, A. A.
1Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, EH9 3JR Edinburgh, UK. 2 Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland. 3 National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India. 4 Department of Biotechnology, Technische Universitat Berlin, 13353 Berlin, Germany.
The ability of kinetochores (KTs) to maintain stable attachments to dynamic microtubule structures ('straight' during microtubule polymerization and 'curved' during microtubule depolymerisation) is an essential requirement for accurate chromosome segregation. Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules.
… “Cells were imaged using a Nikon ECLIPSE Ti microscope equipped with a CoolLED pE-1 excitation system and a 20x/0.75 air Plan Apo objective (Nikon)”….
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