ArticleNature communications2014
XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- The TOG5 domain of CKAP5 is required to interact with F-actin and promote microtubule advancement in neurons.Molecular biology of the cell · 2024Article
- MOR1/MAP215 acts synergistically with katanin to control cell division and anisotropic cell elongation in Arabidopsis.The Plant cell · 2022Article
- Centrosome-dependent microtubule modifications set the conditions for axon formation.Cell reports · 2022Article
- Human Cytomegalovirus Exploits TACC3 To Control Microtubule Dynamics and Late Stages of Infection.Journal of virology · 2021Article
- Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.PLoS genetics · 2021Article
- Investigating the impact of the phosphorylation status of tyrosine residues within the TACC domain of TACC3 on microtubule behavior during axon growth and guidance.Cytoskeleton (Hoboken, N.J.) · 2020Article
- TACC3 Regulates Microtubule Plus-End Dynamics and Cargo Transport in Interphase Cells.Cell reports · 2020Article
- XMAP215 promotes microtubule-F-actin interactions to regulate growth cone microtubules during axon guidance inJournal of cell science · 2019Article
- Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument.Journal of applied crystallography · 2018Article
- The microtubule plus-end-tracking protein TACC3 promotes persistent axon outgrowth and mediates responses to axon guidance signals during development.Neural development · 2017Article
- TACC3-ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation.Biology open · 2015Article
Corrections and comments
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Authors and funding
13 authors at 8 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
chTOG is a conserved microtubule polymerase that catalyses the addition of tubulin dimers to promote microtubule growth. chTOG interacts with TACC3, a member of the transforming acidic coiled-coil (TACC) family. Here we analyse their association using the Xenopus homologues, XTACC3 (TACC3) and XMAP215 (chTOG), dissecting the mechanism by which their interaction promotes microtubule elongation during spindle assembly. Using SAXS, we show that the TACC domain (TD) is an elongated structure that mediates the interaction with the C terminus of XMAP215. Our data suggest that one TD and two XMAP215 molecules associate to form a four-helix coiled-coil complex. A hybrid methods approach was used to define the precise regions of the TACC heptad repeat and the XMAP215 C terminus required for assembly and functioning of the complex. We show that XTACC3 can induce the recruitment of larger amounts of XMAP215 by increasing its local concentration, thereby promoting efficient microtubule elongation during mitosis.
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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.