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Structure. 2017 Jun 6;25(6):924-932.e4. doi: 10.1016/j.str.2017.04.010. Epub 2017 May 25.

Short Linear Sequence Motif LxxPTPh Targets Diverse Proteins to Growing Microtubule Ends.

Author information

1
Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
2
Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, the Netherlands.
3
Institut für Medizinische Immunologie, Charité-Universitätsmedizin Berlin, Leibniz-Institut für Molekulare Pharmakologie, 10117 Berlin, Germany.
4
Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland. Electronic address: michel.steinmetz@psi.ch.

Abstract

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.

KEYWORDS:

X-ray crystallography; end-binding proteins; linear motif; microtubule plus-end tracking proteins; molecular mechanism; structure-function relationship

PMID:
28552577
DOI:
10.1016/j.str.2017.04.010
[Indexed for MEDLINE]
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