{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T03:17:52Z","timestamp":1775531872869,"version":"3.50.1"},"reference-count":39,"publisher":"Rockefeller University Press","issue":"7","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2008,12,29]]},"abstract":"<jats:p>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\u2013binding 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 \u03b1-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.<\/jats:p>","DOI":"10.1083\/jcb.200809190","type":"journal-article","created":{"date-parts":[[2008,12,29]],"date-time":"2008-12-29T12:41:32Z","timestamp":1230554492000},"page":"1223-1233","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":265,"title":["CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1\/tubulin-binding sites"],"prefix":"10.1083","volume":"183","author":[{"given":"Peter","family":"Bieling","sequence":"first","affiliation":[{"name":"1European Molecular Biology Laboratory, Cell Biology and Biophysics Unit, 69117 Heidelberg, Germany"}]},{"given":"Stefanie","family":"Kandels-Lewis","sequence":"additional","affiliation":[{"name":"1European Molecular Biology Laboratory, Cell Biology and Biophysics Unit, 69117 Heidelberg, Germany"}]},{"given":"Ivo A.","family":"Telley","sequence":"additional","affiliation":[{"name":"1European Molecular Biology Laboratory, Cell Biology and Biophysics Unit, 69117 Heidelberg, Germany"}]},{"given":"Juliette","family":"van Dijk","sequence":"additional","affiliation":[{"name":"2Centre de Recherche de Biochimie Macromole\u0301culaire, Universite\u0301 Montpellier 2 and 1, Centre National de la Recherche Scientifique, 34293 Montpellier, France"}]},{"given":"Carsten","family":"Janke","sequence":"additional","affiliation":[{"name":"2Centre de Recherche de Biochimie Macromole\u0301culaire, Universite\u0301 Montpellier 2 and 1, Centre National de la Recherche Scientifique, 34293 Montpellier, France"}]},{"given":"Thomas","family":"Surrey","sequence":"additional","affiliation":[{"name":"1European Molecular Biology Laboratory, Cell Biology and Biophysics Unit, 69117 Heidelberg, Germany"}]}],"member":"291","published-online":{"date-parts":[[2008,12,22]]},"reference":[{"key":"2023072911311916000_BIB1","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/nrm2369","volume":"9","year":"2008","journal-title":"Nat. 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