ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 115 citations in OpenAlex.
- A single-component optogenetic toolkit for reversible visualization and programmable control of microtubule dynamics.Cell reports methods · 2026Article
- CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026Article
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- SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026Article
- CLIP2: a novel functional player in AQP5 trafficking dynamics and implications for Sjögren's disease.Cell communication and signaling : CCS · 2025Article
- Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.bioRxiv : the preprint server for biology · 2025Article
- EB-SUN, a new microtubule plus-end tracking protein inMolecular biology of the cell · 2024Article
- EB-SUN, a New Microtubule Plus-End Tracking Protein inbioRxiv : the preprint server for biology · 2024Article
- EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules.Current biology : CB · 2022Article
- The CLIP-170 N-terminal domain binds directly to both F-actin and microtubules in a mutually exclusive manner.The Journal of biological chemistry · 2022Article
- α-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics.Developmental cell · 2021Article
- Article
- Genetically encoded live-cell sensor for tyrosinated microtubules.The Journal of cell biology · 2020Article
- Arsenic trioxide disturbs the LIS1/NDEL1/dynein microtubule dynamic complex by disrupting the CLIP170 zinc finger in head and neck cancer.Toxicology and applied pharmacology · 2020Article
- Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue.The Journal of cell biology · 2020Article
- Mapping multivalency in the CLIP-170-EB1 microtubule plus-end complex.The Journal of biological chemistry · 2019Article
- The Microtubule-Associated Protein IQ67 DOMAIN5 Modulates Microtubule Dynamics and Pavement Cell Shape.Plant physiology · 2018Article
- Motor axon navigation relies on Fidgetin-like 1-driven microtubule plus end dynamics.The Journal of cell biology · 2018Article
- Poly(ADP-ribose) mediates asymmetric division of mouse oocyte.Cell research · 2018Article
- Tubulin Post-Translational Modifications and Microtubule Dynamics.International journal of molecular sciences · 2017Review
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytoplasmic linker protein 170 (CLIP-170) is a prototype of the plus end-tracking proteins that regulate microtubule dynamics, but it is obscure how CLIP-170 recognizes the microtubule plus end and contributes to polymerization rescue. Crystallographic, NMR, and mutation studies of two tandem cytoskeleton-associated protein glycine-rich (CAP-Gly) domains of CLIP-170, CAP-Gly-1 and CAP-Gly-2, revealed positively charged basic grooves of both CAP-Gly domains for tubulin binding, whereas the CAP-Gly-2 domain possesses a more basic groove and directly binds the EExEEY/F motif of the C-terminal acidic-tail ends of alpha-tubulin. Notably, the p150(Glued) CAP-Gly domain that is furnished with a less positively charged surface only weakly interacts with the alpha-tubulin acidic tail. Mutation studies showed that this acidic sextette motif is the minimum region for CAP-Gly binding. The C-terminal zinc knuckle domains of CLIP-170 bind the basic groove to inhibit the binding to the acidic tails. These results provide a structural basis for the proposed CLIP-170 copolymerization with tubulin on the microtubule plus end. CLIP-170 strongly binds the acidic tails of EB1 as well as those of alpha-tubulins, indicating that EB1 localized at the plus end contributes to CLIP-170 recruitment to the plus end. We suggest that CLIP-170 stimulates microtubule polymerization and/or nucleation by neutralizing the negative charges of tubulins with the highly positive charges of the CLIP-170 CAP-Gly domains. Once CLIP-170 binds microtubule, the released zinc knuckle domain may serve to recruit dynein to the plus end by interacting with p150(Glued) and LIS1. Thus, our structures provide the structural basis for the specific dynein loading on the microtubule plus end.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.