ArticleProceedings of the National Academy of Sciences of the United States of America2011
XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed, 160 citations in OpenAlex.
- Article
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 2026Article
- To Be or Not to Be an Oocyte: Msps/XMAP215 Controls Oocyte Cell Fate in thebioRxiv : the preprint server for biology · 2026Article
- Insights into Microtubule Nucleation at the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Stu2 performs an essential kinetochore function independent of its microtubule polymerase activity.The Journal of cell biology · 2025Article
- A network of interacting ciliary tip proteins with opposing activities imparts slow and processive microtubule growth.Nature structural & molecular biology · 2025Article
- Functional specificity in biomolecular condensates revealed by genetic complementation.Nature reviews. Genetics · 2025Review
- Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends.The Journal of cell biology · 2025Article
- The TOG5 domain of CKAP5 is required to interact with F-actin and promote microtubule advancement in neurons.Molecular biology of the cell · 2024Article
- Mechanism of how the universal module XMAP215 γ-TuRC nucleates microtubules.bioRxiv : the preprint server for biology · 2024Article
- A divergent tumor overexpressed gene domain and oligomerization contribute to SPIRAL2 function in stabilizing microtubule minus ends.The Plant cell · 2024Article
- CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC.Nature cell biology · 2024Article
- CKAP5 enables formation of persistent actin bundles templated by dynamically instable microtubules.Current biology : CB · 2024Article
- New insights into the functions and regulations of MAP215/MOR1 and katanin, two conserved microtubule-associated proteins in Arabidopsis.Plant signaling & behavior · 2023Article
- Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG.Nature communications · 2023Article
- Beyond the GTP-cap: Elucidating the molecular mechanisms of microtubule catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023Review
- ZYG-9ch-TOG promotes the stability of acentrosomal poles via regulation of spindle microtubules in C. elegans oocyte meiosis.PLoS genetics · 2022Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
46 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
XMAP215/Dis1 family proteins positively regulate microtubule growth. Repeats at their N termini, called TOG domains, are important for this function. While TOG domains directly bind tubulin dimers, it is unclear how this interaction translates to polymerase activity. Understanding the functional roles of TOG domains is further complicated by the fact that the number of these domains present in the proteins of different species varies. Here, we take advantage of a recent crystal structure of the third TOG domain from Caenorhabditis elegans, Zyg9, and mutate key residues in each TOG domain of XMAP215 that are predicted to be important for interaction with the tubulin heterodimer. We determined the contributions of the individual TOG domains to microtubule growth. We show that the TOG domains are absolutely required to bind free tubulin and that the domains differentially contribute to XMAP215's overall affinity for free tubulin. The mutants' overall affinity for free tubulin correlates well with polymerase activity. Furthermore, we demonstrate that an additional basic region is important for targeting to the microtubule lattice and is critical for XMAP215 to function at physiological concentrations. Using this information, we have engineered a "bonsai" protein, with two TOG domains and a basic region, that has almost full polymerase activity.
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