ArticleThe Journal of cell biology1999
Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 58 citations in OpenAlex.
- 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
- Interaction of Colchicine-Site Ligands With the Blood Cell-Specific Isotype of β-Tubulin-Notable Affinity for Benzimidazoles.Frontiers in cell and developmental biology · 2022Article
- The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans.Virulence · 2018Article
- 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
- Article
- Three-dimensional structure of CAP-gly domain of mammalian dynactin determined by magic angle spinning NMR spectroscopy: conformational plasticity and interactions with end-binding protein EB1.Journal of molecular biology · 2013Article
- 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
- Autoinhibition of TBCB regulates EB1-mediated microtubule dynamics.Cellular and molecular life sciences : CMLS · 2013Article
- Drosophila tubulin-binding cofactor B is required for microtubule network formation and for cell polarity.Molecular biology of the cell · 2012Article
- Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress.Cellular and molecular life sciences : CMLS · 2010Article
- CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin.The EMBO journal · 2010Article
- Stu1p is physically associated with beta-tubulin and is required for structural integrity of the mitotic spindle.Molecular biology of the cell · 2002Article
- Protection from free beta-tubulin by the beta-tubulin binding protein Rbl2p.Molecular and cellular biology · 2002Article
- The cofactor-dependent pathways for alpha- and beta-tubulins in microtubule biogenesis are functionally different in fission yeast.Genetics · 2000Article
- Function of tubulin binding proteins in vivo.Genetics · 2000Article
- ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin.The Journal of cell biology · 2000Article
- Structure-function relationships in yeast tubulins.Molecular biology of the cell · 2000Article
- Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast.Molecular biology of the cell · 1999Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Tubulin is a heterodimer of alpha- and beta-tubulin polypeptides. Assembly of the tubulin heterodimer in vitro requires the CCT chaperonin complex, and a set of five proteins referred to as the tubulin cofactors (Tian, F., Y. Huang, H. Rommelaere, J. Vandekerckhove, C. Ampe, and N.J. Cowan. 1996. Cell. 86:287-296; Tian, G., S.A. Lewis, B. Feierbach, T. Stearns, H. Rommelaere, C. Ampe, and N.J. Cowan. 1997. J. Cell Biol. 138:821-832). We report the characterization of Alf1p, the yeast ortholog of mammalian cofactor B. Alf1p interacts with alpha-tubulin in both two-hybrid and immunoprecipitation assays. Alf1p and cofactor B contain a single CLIP-170 domain, which is found in several microtubule-associated proteins. Mutation of the CLIP-170 domain in Alf1p disrupts the interaction with alpha-tubulin. Mutations in alpha-tubulin that disrupt the interaction with Alf1p map to a domain on the cytoplasmic face of alpha-tubulin; this domain is distinct from the region of interaction between alpha-tubulin and beta-tubulin. Alf1p-green fluorescent protein (GFP) is able to associate with microtubules in vivo, and this localization is abolished either by mutation of the CLIP-170 domain in Alf1p, or by mutation of the Alf1p-binding domain in alpha-tubulin. Analysis of double mutants constructed between null alleles of ALF1 and PAC2, which encodes the other yeast alpha-tubulin cofactor, suggests that Alf1p and Pac2p act in the same pathway leading to functional alpha-tubulin. The phenotype of overexpression of ALF1 suggests that Alf1p can act to sequester alpha-tubulin from interaction with beta-tubulin, raising the possibility that it plays a regulatory role in the formation of the tubulin heterodimer.
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