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

Friese, A., Faesen, A. C., in 't Veld, P. J. H., Fischbock, J., Prumbaum, D., Petrovic, A., et al. (2016). Molecular requirements for the inter-subunit interaction and kinetochore recruitment of SKAP and Astrin. Nature Communications, 11: 11407. doi:10.1038/ncomms11407.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C696-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C6A1-4
Genre: Journal Article

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 Creators:
Friese, A., Author
Faesen, A. C.1, Author              
in 't Veld, P. J. H., Author
Fischbock, J., Author
Prumbaum, D., Author
Petrovic, A., Author
Raunser, S., Author
Herzog, F., Author
Musacchio, A., Author
Affiliations:
1Research Group Biochemistry of Signal Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2466695              

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 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.

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Language(s): eng - English
 Dates: 2016-04-20
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms11407
 Degree: -

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Title: Nature Communications
Source Genre: Journal
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Pages: 12 Volume / Issue: 11 Sequence Number: 11407 Start / End Page: - Identifier: -