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CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites

The microtubule cytoskeleton is crucial for the internal organization of eukaryotic cells. Several microtubule-associated proteins link microtubules to subcellular structures. A subclass of these proteins, the plus end–binding proteins (+TIPs), selectively binds to the growing plus ends of microtubu...

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Autores principales: Bieling, Peter, Kandels-Lewis, Stefanie, Telley, Ivo A., van Dijk, Juliette, Janke, Carsten, Surrey, Thomas
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2606963/
https://www.ncbi.nlm.nih.gov/pubmed/19103809
http://dx.doi.org/10.1083/jcb.200809190
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author Bieling, Peter
Kandels-Lewis, Stefanie
Telley, Ivo A.
van Dijk, Juliette
Janke, Carsten
Surrey, Thomas
author_facet Bieling, Peter
Kandels-Lewis, Stefanie
Telley, Ivo A.
van Dijk, Juliette
Janke, Carsten
Surrey, Thomas
author_sort Bieling, Peter
collection PubMed
description The microtubule cytoskeleton is crucial for the internal organization of eukaryotic cells. Several microtubule-associated proteins link microtubules to subcellular structures. A subclass of these proteins, the plus end–binding proteins (+TIPs), selectively binds to the growing plus ends of microtubules. Here, we reconstitute a vertebrate plus end tracking system composed of the most prominent +TIPs, end-binding protein 1 (EB1) and CLIP-170, in vitro and dissect their end-tracking mechanism. We find that EB1 autonomously recognizes specific binding sites present at growing microtubule ends. In contrast, CLIP-170 does not end-track by itself but requires EB1. CLIP-170 recognizes and turns over rapidly on composite binding sites constituted by end-accumulated EB1 and tyrosinated α-tubulin. In contrast to its fission yeast orthologue Tip1, dynamic end tracking of CLIP-170 does not require the activity of a molecular motor. Our results demonstrate evolutionary diversity of the plus end recognition mechanism of CLIP-170 family members, whereas the autonomous end-tracking mechanism of EB family members is conserved.
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spelling pubmed-26069632009-06-29 CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites Bieling, Peter Kandels-Lewis, Stefanie Telley, Ivo A. van Dijk, Juliette Janke, Carsten Surrey, Thomas J Cell Biol Research Articles The microtubule cytoskeleton is crucial for the internal organization of eukaryotic cells. Several microtubule-associated proteins link microtubules to subcellular structures. A subclass of these proteins, the plus end–binding proteins (+TIPs), selectively binds to the growing plus ends of microtubules. Here, we reconstitute a vertebrate plus end tracking system composed of the most prominent +TIPs, end-binding protein 1 (EB1) and CLIP-170, in vitro and dissect their end-tracking mechanism. We find that EB1 autonomously recognizes specific binding sites present at growing microtubule ends. In contrast, CLIP-170 does not end-track by itself but requires EB1. CLIP-170 recognizes and turns over rapidly on composite binding sites constituted by end-accumulated EB1 and tyrosinated α-tubulin. In contrast to its fission yeast orthologue Tip1, dynamic end tracking of CLIP-170 does not require the activity of a molecular motor. Our results demonstrate evolutionary diversity of the plus end recognition mechanism of CLIP-170 family members, whereas the autonomous end-tracking mechanism of EB family members is conserved. The Rockefeller University Press 2008-12-29 /pmc/articles/PMC2606963/ /pubmed/19103809 http://dx.doi.org/10.1083/jcb.200809190 Text en © 2008 Bieling et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Bieling, Peter
Kandels-Lewis, Stefanie
Telley, Ivo A.
van Dijk, Juliette
Janke, Carsten
Surrey, Thomas
CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
title CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
title_full CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
title_fullStr CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
title_full_unstemmed CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
title_short CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
title_sort clip-170 tracks growing microtubule ends by dynamically recognizing composite eb1/tubulin-binding sites
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2606963/
https://www.ncbi.nlm.nih.gov/pubmed/19103809
http://dx.doi.org/10.1083/jcb.200809190
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