ArticleJournal of molecular biology2010
Probing interactions between CLIP-170, EB1, and microtubules.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- KIF20A promotes cervical cancer progression by interacting with CLIP1.Scientific reports · 2026Article
- CLIP2: a novel functional player in AQP5 trafficking dynamics and implications for Sjögren's disease.Cell communication and signaling : CCS · 2025Article
- Phase separation of +TIP networks regulates microtubule dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- 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
- CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engagement.Developmental cell · 2021Article
- α-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics.Developmental cell · 2021Article
- Microtubule-based force generation.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2017Review
- Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins.Cytoskeleton (Hoboken, N.J.) · 2015Review
- Drosophila CLIP-190 and mammalian CLIP-170 display reduced microtubule plus end association in the nervous system.Molecular biology of the cell · 2015Article
- Genome-wide analysis reveals novel and discrete functions for tubulin carboxy-terminal tails.Current biology : CB · 2014Article
- Dynactin subunit p150(Glued) is a neuron-specific anti-catastrophe factor.PLoS biology · 2013Article
- Using MTBindingSim as a tool for experimental planning and interpretation.Methods in cell biology · 2013Article
- The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions.Cytoskeleton (Hoboken, N.J.) · 2012Review
- Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein.BMC evolutionary biology · 2012Article
- PSD-95 alters microtubule dynamics via an association with EB3.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- EB1 is required for spindle symmetry in mammalian mitosis.PloS one · 2011Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Cytoplasmic linker protein 170 (CLIP-170) is a microtubule (MT) plus-end tracking protein (+TIP) that dynamically localizes to the MT plus end and regulates MT dynamics. The mechanisms of these activities remain unclear because the CLIP-170-MT interaction is poorly understood, and even less is known about how CLIP-170 and other +TIPs act together as a network. CLIP-170 binds to the acidic C-terminal tail of alpha-tubulin. However, the observation that CLIP-170 has two CAP-Gly (cytoskeleton-associated protein glycine-rich) motifs and multiple serine-rich regions suggests that a single CLIP-170 molecule has multiple tubulin binding sites, and that these sites might bind to multiple parts of the tubulin dimer. Using a combination of chemical cross-linking and mass spectrometry, we find that CLIP-170 binds to both alpha-tubulin and beta-tubulin, and that binding is not limited to the acidic C-terminal tails. We provide evidence that these additional binding sites include the H12 helices of both alpha-tubulin and beta-tubulin and are significant for CLIP-170 activity. Previous work has shown that CLIP-170 binds to end-binding protein 1 (EB1) via the EB1 C-terminus, which mimics the acidic C-terminal tail of tubulin. We find that CLIP-170 can utilize its multiple tubulin binding sites to bind to EB1 and MT simultaneously. These observations help to explain how CLIP-170 can nucleate MTs and alter MT dynamics, and they contribute to understanding the significance and properties of the +TIP network.
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What OpenQuestion holds
Registered trials
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.