ArticleCurrent biology : CB2018
The XMAP215 Ortholog Alp14 Promotes Microtubule Nucleation in Fission Yeast.
Article in Current biology : CB, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 72 citations in OpenAlex.
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 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
- 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
- New insights into the functions and regulations of MAP215/MOR1 and katanin, two conserved microtubule-associated proteins in Arabidopsis.Plant signaling & behavior · 2023Article
- Multifaceted modes of γ-tubulin complex recruitment and microtubule nucleation at mitotic centrosomes.The Journal of cell biology · 2023Article
- Microtubule nucleation for spindle assembly: one molecule at a time.Trends in biochemical sciences · 2023Review
- Mechanisms underlying spindle assembly and robustness.Nature reviews. Molecular cell biology · 2023Review
- Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG.Nature communications · 2023Article
- Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- MOR1/MAP215 acts synergistically with katanin to control cell division and anisotropic cell elongation in Arabidopsis.The Plant cell · 2022Article
- Review
- Microtubule Anchoring: Attaching Dynamic Polymers to Cellular Structures.Frontiers in cell and developmental biology · 2022Review
- Microtubule-associated proteins promote microtubule generation in the absence of γ-tubulin in human colon cancer cells.The Journal of cell biology · 2021Article
- Human Cytomegalovirus Exploits TACC3 To Control Microtubule Dynamics and Late Stages of Infection.Journal of virology · 2021Article
- Loss of kinesin-8 improves the robustness of the self-assembled spindle in Schizosaccharomyces pombe.Journal of cell science · 2021Article
- Autoinhibition of Cnn binding to γ-TuRCs prevents ectopic microtubule nucleation and cell division defects.The Journal of cell biology · 2021Article
- Molecular insight into how γ-TuRC makes microtubules.Journal of cell science · 2021Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The organization and number of microtubules (MTs) in a cell depend on the proper regulation of MT nucleation. Currently, the mechanism of nucleation is the most poorly understood aspect of MT dynamics. XMAP215/chTOG/Alp14/Stu2 proteins are MT polymerases that stimulate MT polymerization at MT plus ends by binding and releasing tubulin dimers. Although these proteins also localize to MT organizing centers and have nucleating activity in vitro, it is not yet clear whether these proteins participate in MT nucleation in vivo. Here, we demonstrate that in the fission yeast Schizosaccharomyces pombe, the XMAP215 ortholog Alp14 is critical for efficient MT nucleation in vivo. In multiple assays, loss of Alp14 function led to reduced nucleation rate and numbers of interphase MT bundles. Conversely, activation of Alp14 led to increased nucleation frequency. Alp14 associated with Mto1 and γ-tubulin complex components, and artificially targeting Alp14 to the γ-tubulin ring complexes (γ-TuRCs) stimulated nucleation. In imaging individual nucleation events, we found that Alp14 transiently associated with a γ-tubulin particle shortly before the appearance of a new MT. The transforming acidic coiled-coil (TACC) ortholog Alp7 mediated the localization of Alp14 at nucleation sites but not plus ends, and was required for efficient nucleation but not for MT polymerization. Our findings provide the strongest evidence to date that Alp14 serves as a critical MT nucleation factor in vivo. We suggest a model in which Alp14 associates with the γ-tubulin complex in an Alp7-dependent manner to facilitate the assembly or stabilization of the nascent MT.
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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.