The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
Open accessAbstract
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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Cites
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The tubulin code and its role in controlling microtubule properties and functions
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Self-citationAn EB1-binding motif acts as a microtubule tip localization signal
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The tubulin code: Molecular components, readout mechanisms, and functions
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Self-citationMammalian end binding proteins control persistent microtubule growth
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Metadata
- Authors
- Bieling, P., Kandels-Lewis, S., Telley, I. A., van Dijk, J., Janke, C., & Surrey, T.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2008-12-22
- Volume
- 183
- Issue
- 7
- Pages
- 1223-1233
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2054084181
- Cited by
- 287
- References
- 39
- FWCI
- 8.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
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