ArticleMolecular biology of the cell1999
Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 72 citations in OpenAlex.
- Cryo-EM structures of the tubulin cofactors reveal the molecular basis of alpha/beta-tubulin biogenesis.Nature communications · 2025Article
- 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
- The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans.Virulence · 2018Article
- Nucleotide Binding to ARL2 in the TBCD∙ARL2∙β-Tubulin Complex Drives Conformational Changes in β-Tubulin.Journal of molecular biology · 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
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- The dual role of fission yeast Tbc1/cofactor C orchestrates microtubule homeostasis in tubulin folding and acts as a GAP for GTPase Alp41/Arl2.Molecular biology of the cell · 2013Article
- Drosophila tubulin-binding cofactor B is required for microtubule network formation and for cell polarity.Molecular biology of the cell · 2012Article
- Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress.Cellular and molecular life sciences : CMLS · 2010Article
- Tubulin heterodimers remain functional for one cell cycle after the inactivation of tubulin-folding cofactor D in fission yeast cells.Yeast (Chichester, England) · 2009Article
- Chromosome segregation in fission yeast with mutations in the tubulin folding cofactor D.Current genetics · 2006Article
- Cryptic out-of-frame translational initiation of TBCE rescues tubulin formation in compound heterozygous HRD.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- p21-activated kinase 1 regulates microtubule dynamics by phosphorylating tubulin cofactor B.Molecular and cellular biology · 2005Article
- Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization.BMC bioinformatics · 2003Article
- Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease.The Journal of cell biology · 2002Article
- The Arabidopsis PILZ group genes encode tubulin-folding cofactor orthologs required for cell division but not cell growth.Genes & development · 2002Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe the isolation of fission yeast homologues of tubulin-folding cofactors B (Alp11) and E (Alp21), which are essential for cell viability and the maintenance of microtubules. Alp11(B) contains the glycine-rich motif (the CLIP-170 domain) involved in microtubular functions, whereas, unlike mammalian cofactor E, Alp21(E) does not. Both mammalian and yeast cofactor E, however, do contain leucine-rich repeats. Immunoprecipitation analysis shows that Alp11(B) interacts with both alpha-tubulin and Alp21(E), but not with the cofactor D homologue Alp1, whereas Alp21(E) also interacts with Alp1(D). The cellular amount of alpha-tubulin is decreased in both alp1 and alp11 mutants. Overproduction of Alp11(B) results in cell lethality and the disappearance of microtubules, which is rescued by co-overproduction of alpha-tubulin. Both full-length Alp11(B) and the C-terminal third containing the CLIP-170 domain localize in the cytoplasm, and this domain is required for efficient binding to alpha-tubulin. Deletion of alp11 is suppressed by multicopy plasmids containing either alp21(+) or alp1(+), whereas alp21 deletion is rescued by overexpression of alp1(+) but not alp11(+). Finally, the alp1 mutant is not complemented by either alp11(+) or alp21(+). The results suggest that cofactors operate in a linear pathway (Alp11(B)-Alp21(E)-Alp1(D)), each with distinct roles.
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