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Structure-Function Relationship of the Bik1-Bim1 Complex.
- Source :
-
Structure (London, England : 1993) [Structure] 2018 Apr 03; Vol. 26 (4), pp. 607-618.e4. Date of Electronic Publication: 2018 Mar 22. - Publication Year :
- 2018
-
Abstract
- In budding yeast, the microtubule plus-end tracking proteins Bik1 (CLIP-170) and Bim1 (EB1) form a complex that interacts with partners involved in spindle positioning, including Stu2 and Kar9. Here, we show that the CAP-Gly and coiled-coil domains of Bik1 interact with the C-terminal ETF peptide of Bim1 and the C-terminal tail region of Stu2, respectively. The crystal structures of the CAP-Gly domain of Bik1 (Bik1CG) alone and in complex with an ETF peptide revealed unique, functionally relevant CAP-Gly elements, establishing Bik1CG as a specific C-terminal phenylalanine recognition domain. Unlike the mammalian CLIP-170-EB1 complex, Bik1-Bim1 forms ternary complexes with the EB1-binding motifs SxIP and LxxPTPh, which are present in diverse proteins, including Kar9. Perturbation of the Bik1-Bim1 interaction in vivo affected Bik1 localization and astral microtubule length. Our results provide insight into the role of the Bik1-Bim1 interaction for cell division, and demonstrate that the CLIP-170-EB1 module is evolutionarily flexible.<br /> (Copyright © 2018 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Binding Sites
Cell Cycle Proteins genetics
Cell Cycle Proteins metabolism
Cell Division
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli genetics
Escherichia coli metabolism
Evolution, Molecular
Gene Expression
Genetic Vectors chemistry
Genetic Vectors metabolism
Microtubule Proteins genetics
Microtubule Proteins metabolism
Microtubule-Associated Proteins genetics
Microtubule-Associated Proteins metabolism
Microtubules chemistry
Microtubules ultrastructure
Models, Molecular
Nuclear Proteins genetics
Nuclear Proteins metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae ultrastructure
Saccharomyces cerevisiae Proteins genetics
Saccharomyces cerevisiae Proteins metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Spindle Apparatus chemistry
Spindle Apparatus ultrastructure
Structure-Activity Relationship
Cell Cycle Proteins chemistry
Microtubule Proteins chemistry
Microtubule-Associated Proteins chemistry
Nuclear Proteins chemistry
Saccharomyces cerevisiae chemistry
Saccharomyces cerevisiae Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 26
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 29576319
- Full Text :
- https://doi.org/10.1016/j.str.2018.03.003