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Manatschal C, Farcas AM, Degen MS, et al. Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning. Mol Biol Cell. 2016;doi: 10.1091/mbc.E16-07-0552.
Manatschal, C., Farcas, A. M., Degen, M. S., Bayer, M., Kumar, A., Landgraf, C., Volkmer, R., Barral, Y., & Steinmetz, M. O. (2016). Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning. Molecular biology of the cell, . https://doi.org/10.1091/mbc.E16-07-0552
Manatschal, Cristina, et al. "Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning." Molecular biology of the cell vol. (2016). doi: https://doi.org/10.1091/mbc.E16-07-0552
Manatschal C, Farcas AM, Degen MS, Bayer M, Kumar A, Landgraf C, Volkmer R, Barral Y, Steinmetz MO. Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning. Mol Biol Cell. 2016 Sep 28; doi: 10.1091/mbc.E16-07-0552. Epub 2016 Sep 28. PMID: 27682587; PMCID: PMC5170556.
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Mol Biol Cell. 2016 Sep 28; doi: 10.1091/mbc.E16-07-0552. Epub 2016 Sep 28.

Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning.

Molecular biology of the cell

Cristina Manatschal, Ana-Maria Farcas, Miriam Steiner Degen, Mathias Bayer, Anil Kumar, Christiane Landgraf, Rudolf Volkmer, Yves Barral, Michel O Steinmetz

Affiliations

  1. Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen PSI, Switzerland.
  2. Institute of Biochemistry, Biology Department, ETH Zürich, Zürich, Switzerland.
  3. Institut für Medizinische Immunologie, Charité-Universitätsmedizin Berlin, Berlin, Germany.
  4. Institute of Biochemistry, Biology Department, ETH Zürich, Zürich, Switzerland [email protected] [email protected].
  5. Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen PSI, Switzerland [email protected] [email protected].

PMID: 27682587 PMCID: PMC5170556 DOI: 10.1091/mbc.E16-07-0552

Abstract

The Kar9 pathway promotes nuclear fusion during mating and spindle alignment during metaphase in budding yeast. How Kar9 supports the different outcome of these two divergent processes is an open question. Here, we show that three sites in the C-terminal disordered domain of Kar9 mediate tight Kar9 interaction with the C-terminal dimerization domain of Bim1 (EB1 orthologue). Site1 and Site2 contain SxIP motifs; however, Site3 defines a novel type of EB1-binding site. Whereas Site2 and Site3 mediate Kar9 recruitment to microtubule tips, nuclear movement and karyogamy, solely Site2 functions in spindle positioning during metaphase. Site1 in turn plays an inhibitory role during mating. Additionally, the Kar9-Bim1 complex is involved in microtubule-independent activities during mating. Together, our data reveal how multiple and partially redundant EB1-binding sites provide a microtubule-associated protein with the means to modulate its biochemical properties to promote different molecular processes during cell proliferation and differentiation.

© 2016 by The American Society for Cell Biology.

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