ArticleThe EMBO journal2001
XMAP215 regulates microtubule dynamics through two distinct domains.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 2026Article
- Interplay between microtubule interactome, myonuclei mechanotransduction, and positioning in myopathies.Nucleus (Austin, Tex.) · 2025Review
- Mechanism of how the universal module XMAP215 γ-TuRC nucleates microtubules.bioRxiv : the preprint server for biology · 2024Article
- TACC3-ch-TOG interaction regulates spindle microtubule assembly by controlling centrosomal recruitment of γ-TuRC.Bioscience reports · 2023Article
- Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG.Nature communications · 2023Article
- The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle.Open biology · 2020Review
- In vivo mitotic spindle scaling can be modulated by changing the levels of a single protein: the microtubule polymerase XMAP215.Molecular biology of the cell · 2018Article
- XMAP215 is a microtubule nucleation factor that functions synergistically with the γ-tubulin ring complex.Nature cell biology · 2018Article
- TOG-tubulin binding specificity promotes microtubule dynamics and mitotic spindle formation.The Journal of cell biology · 2017Article
- The viral protein gp120 decreases the acetylation of neuronal tubulin: potential mechanism of neurotoxicity.Journal of neurochemistry · 2017Article
- XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation.Nature communications · 2014Article
- The XMAP215 family drives microtubule polymerization using a structurally diverse TOG array.Molecular biology of the cell · 2014Article
- The centrosomal adaptor TACC3 and the microtubule polymerase chTOG interact via defined C-terminal subdomains in an Aurora-A kinase-independent manner.The Journal of biological chemistry · 2014Article
- The microtubule lattice and plus-end association of Drosophila Mini spindles is spatially regulated to fine-tune microtubule dynamics.Molecular biology of the cell · 2011Article
- Microtubule assembly in meiotic extract requires glycogen.Molecular biology of the cell · 2011Article
- XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- GDP-tubulin incorporation into growing microtubules modulates polymer stability.The Journal of biological chemistry · 2010Article
- Xenopus meiotic microtubule-associated interactome.PloS one · 2010Article
- The transcriptional repressor Kaiso localizes at the mitotic spindle and is a constituent of the pericentriolar material.PloS one · 2010Article
- XMAP215-EB1 interaction is required for proper spindle assembly and chromosome segregation in Xenopus egg extract.Molecular biology of the cell · 2009Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
XMAP215 belongs to a family of proteins involved in the regulation of microtubule dynamics. In this study we analyze the function of different parts of XMAP215 in vivo and in Xenopus egg extracts. XMAP215 has been divided into three fragments, FrN, FrM and FrC (for N-terminal, middle and C-terminal, respectively). FrN co-localizes with microtubules in egg extracts but not in cells, FrC co- localizes with microtubules and centrosomes both in egg extracts and in cells, while FrM does not co- localize with either centrosomes or microtubules. In Xenopus egg extracts, FrN stimulates microtubule growth at plus-ends by inhibiting catastrophes, while FrM has no effect, and FrC suppresses microtubule growth by promoting catastrophes. Our results suggest that XMAP215 is targeted to centrosomes and microtubules mainly through its C-terminal domain, while the evolutionarily conserved N-terminal domain contains its microtubule-stabilizing activity.
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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.