ArticleThe Journal of cell biology2003
Identification of XMAP215 as a microtubule-destabilizing factor in Xenopus egg extract by biochemical purification.
Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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.
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Who cites it
54 citing papers in PubMed, 102 citations in OpenAlex.
- CKAP5 stabilizes CENP-E at kinetochores by regulating microtubule-chromosome attachments.EMBO reports · 2024Article
- CLASP2 recognizes tubulins exposed at the microtubule plus-end in a nucleotide state-sensitive manner.Science advances · 2023Article
- C. elegans XMAP215/ZYG-9 and TACC/TAC-1 act at multiple times during oocyte meiotic spindle assembly and promote both spindle pole coalescence and stability.PLoS genetics · 2023Article
- Beyond the GTP-cap: Elucidating the molecular mechanisms of microtubule catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Fission yeast Dis1 is an unconventional TOG/XMAP215 that induces microtubule catastrophe to drive chromosome pulling.Communications biology · 2022Article
- The TOG protein Stu2 is regulated by acetylation.PLoS genetics · 2022Article
- Article
- Microtubule assembly and pole coalescence: early steps inBiology open · 2020Article
- Mapping the kinetochore MAP functions required for stabilizing microtubule attachments to chromosomes during metaphase.Cytoskeleton (Hoboken, N.J.) · 2019Review
- Microtubule polymerase and processive plus-end tracking functions originate from distinct features within TOG domain arrays.Molecular biology of the cell · 2019Article
- The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Probing the biology of cell boundary conditions through confinement of Xenopus cell-free cytoplasmic extracts.Genesis (New York, N.Y. : 2000) · 2017Review
- An unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation.Journal of cell science · 2016Article
- Article
- Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism.Scientific reports · 2016Article
- Ahead of the Curve: New Insights into Microtubule Dynamics.F1000Research · 2016Review
- Kinesin-5 is a microtubule polymerase.Nature communications · 2015Article
- TTBK2 with EB1/3 regulates microtubule dynamics in migrating cells through KIF2A phosphorylation.The Journal of cell biology · 2015Article
- A sensitised RNAi screen reveals a ch-TOG genetic interaction network required for spindle assembly.Scientific reports · 2015Article
- TOG Proteins Are Spatially Regulated by Rac-GSK3β to Control Interphase Microtubule Dynamics.PloS one · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Microtubules (MTs) polymerized with GMPCPP, a slowly hydrolyzable GTP analogue, are stable in buffer but are rapidly depolymerized in Xenopus egg extracts. This depolymerization is independent of three previously identified MT destabilizers (Op18, katanin, and XKCM1/KinI). We purified the factor responsible for this novel depolymerizing activity using biochemical fractionation and a visual activity assay and identified it as XMAP215, previously identified as a prominent MT growth-promoting protein in Xenopus extracts. Consistent with the purification results, we find that XMAP215 is necessary for GMPCPP-MT destabilization in extracts and that recombinant full-length XMAP215 as well as an NH2-terminal fragment have depolymerizing activity in vitro. Stimulation of depolymerization is specific for the MT plus end. These results provide evidence for a robust MT-destabilizing activity intrinsic to this microtubule-associated protein and suggest that destabilization may be part of its essential biochemical functions. We propose that the substrate in our assay, GMPCPP-stabilized MTs, serves as a model for the pause state of MT ends and that the multiple activities of XMAP215 are unified by a mechanism of antagonizing MT pauses.
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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.