ArticleThe Journal of cell biology1997
Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 196 citations in OpenAlex.
- In silico analysis of TUBA4A mutations in Amyotrophic Lateral Sclerosis to define mechanisms of microtubule disintegration.Scientific reports · 2023Article
- Decreased tubulin-binding cofactor B was involved in the formation disorder of nascent astrocyte processes by regulating microtubule plus-end growth through binding with end-binding proteins 1 and 3 after chronic alcohol exposure.Frontiers in cellular neuroscience · 2022Article
- Reconstituting Microtubules: A Decades-Long Effort From Building Block Identification to the Generation of Recombinant α/β-Tubulin.Frontiers in cell and developmental biology · 2022Review
- Skeletal muscle proteomes reveal downregulation of mitochondrial proteins in transition from prediabetes into type 2 diabetes.iScience · 2021Article
- Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly.Science (New York, N.Y.) · 2021Article
- Mechanisms of Taxane ResistanceCancers · 2020Review
- Microtubule dynamics at low temperature: evidence that tubulin recycling limits assembly.Molecular biology of the cell · 2020Article
- β-tubulin carboxy-terminal tails exhibit isotype-specific effects on microtubule dynamics in human gene-edited cells.Life science alliance · 2018Article
- Nucleotide Binding to ARL2 in the TBCD∙ARL2∙β-Tubulin Complex Drives Conformational Changes in β-Tubulin.Journal of molecular biology · 2017Article
- HILI destabilizes microtubules by suppressing phosphorylation and Gigaxonin-mediated degradation of TBCB.Scientific reports · 2017Article
- A Trimer Consisting of the Tubulin-specific Chaperone D (TBCD), Regulatory GTPase ARL2, and β-Tubulin Is Required for Maintaining the Microtubule Network.The Journal of biological chemistry · 2017Article
- Revisiting the tubulin cofactors and Arl2 in the regulation of soluble αβ-tubulin pools and their effect on microtubule dynamics.Molecular biology of the cell · 2017Article
- Infantile neurodegenerative disorder associated with mutations in TBCD, an essential gene in the tubulin heterodimer assembly pathway.Human molecular genetics · 2016Article
- Biallelic TBCD Mutations Cause Early-Onset Neurodegenerative Encephalopathy.American journal of human genetics · 2016Article
- Higher order signaling: ARL2 as regulator of both mitochondrial fusion and microtubule dynamics allows integration of 2 essential cell functions.Small GTPases · 2016Review
- The cytoskeletal arrangements necessary to neurogenesis.Oncotarget · 2016Review
- Arl2- and Msps-dependent microtubule growth governs asymmetric division.The Journal of cell biology · 2016Article
- Novel α-tubulin mutation disrupts neural development and tubulin proteostasis.Developmental biology · 2016Article
- Article
- Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast.Molecular biology of the cell · 2015Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The production of native alpha/beta tubulin heterodimer in vitro depends on the action of cytosolic chaperonin and several protein cofactors. We previously showed that four such cofactors (termed A, C, D, and E) together with native tubulin act on beta-tubulin folding intermediates generated by the chaperonin to produce polymerizable tubulin heterodimers. However, this set of cofactors generates native heterodimers only very inefficiently from alpha-tubulin folding intermediates produced by the same chaperonin. Here we describe the isolation, characterization, and genetic analysis of a novel tubulin folding cofactor (cofactor B) that greatly enhances the efficiency of alpha-tubulin folding in vitro. This enabled an integrated study of alpha- and beta-tubulin folding: we find that the pathways leading to the formation of native alpha- and beta-tubulin converge in that the folding of the alpha subunit requires the participation of cofactor complexes containing the beta subunit and vice versa. We also show that sequestration of native alpha-or beta-tubulins by complex formation with cofactors results in the destabilization and decay of the remaining free subunit. These data demonstrate that tubulin folding cofactors function by placing and/or maintaining alpha-and beta-tubulin polypeptides in an activated conformational state required for the formation of native alpha/beta heterodimers, and imply that each subunit provides information necessary for the proper folding of the other.
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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.