Short Linear Sequence Motif LxxPTPh Targets Diverse Proteins to Growing Microtubule Ends.
- Kumar A Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
- Manatschal C Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
- Rai A Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, the Netherlands.
- Grigoriev I Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, the Netherlands.
- Degen MS Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
- Jaussi R Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
- Kretzschmar I Institut für Medizinische Immunologie, Charité-Universitätsmedizin Berlin, Leibniz-Institut für Molekulare Pharmakologie, 10117 Berlin, Germany.
- Prota AE Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
- Volkmer R Institut für Medizinische Immunologie, Charité-Universitätsmedizin Berlin, Leibniz-Institut für Molekulare Pharmakologie, 10117 Berlin, Germany.
- Kammerer RA Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
- Akhmanova A Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, the Netherlands.
- Steinmetz MO Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland. Electronic address: michel.steinmetz@psi.ch.
- 2017-05-30
Published in:
- Structure (London, England : 1993). - 2017
X-ray crystallography
end-binding proteins
linear motif
microtubule plus-end tracking proteins
molecular mechanism
structure-function relationship
Amino Acid Motifs
Animals
Binding Sites
COS Cells
Cell Cycle Proteins
Chlorocebus aethiops
Crystallography, X-Ray
Fluorescence Polarization
Microtubule Proteins
Microtubule-Associated Proteins
Microtubules
Models, Molecular
Nuclear Proteins
Protein Domains
Saccharomyces cerevisiae Proteins
English
Microtubule plus-end tracking proteins (+TIPs) are involved in virtually all microtubule-based processes. End-binding (EB) proteins are considered master regulators of +TIP interaction networks, since they autonomously track growing microtubule ends and recruit a plethora of proteins to this location. Two major EB-interacting elements have been described: CAP-Gly domains and linear SxIP sequence motifs. Here, we identified LxxPTPh as a third EB-binding motif that enables major +TIPs to interact with EBs at microtubule ends. In contrast to EB-SxIP and EB-CAP-Gly, the EB-LxxPTPh binding mode does not depend on the C-terminal tail region of EB. Our study reveals that +TIPs developed additional strategies besides CAP-Gly and SxIP to target EBs at growing microtubule ends. They further provide a unique basis to discover novel +TIPs, and to dissect the role of key interaction nodes and their differential regulation for hierarchical +TIP network organization and function in eukaryotic organisms.
- Language
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- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1016/j.str.2017.04.010
- PMID 28552577
- Persistent URL
- https://sonar.ch/global/documents/888
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