ArticleMolecular and cellular biology1998
Formation and function of the Rbl2p-beta-tubulin complex.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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
11 citing papers in PubMed, 27 citations in OpenAlex.
- Novel α-tubulin mutation disrupts neural development and tubulin proteostasis.Developmental biology · 2016Article
- Article
- The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Faithful chaperones.Cellular and molecular life sciences : CMLS · 2011Review
- TBCD links centriologenesis, spindle microtubule dynamics, and midbody abscission in human cells.PloS one · 2010Article
- Consequences of defective tubulin folding on heterodimer levels, mitosis and spindle morphology in Saccharomyces cerevisiae.Genetics · 2006Article
- Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source.Molecular biology of the cell · 2002Article
- Protection from free beta-tubulin by the beta-tubulin binding protein Rbl2p.Molecular and cellular biology · 2002Article
- Function of tubulin binding proteins in vivo.Genetics · 2000Article
- Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin.The Journal of cell biology · 1999Article
- An alpha-tubulin mutant destabilizes the heterodimer: phenotypic consequences and interactions with tubulin-binding proteins.Molecular biology of the cell · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast protein Rbl2p suppresses the deleterious effects of excess beta-tubulin as efficiently as does alpha-tubulin. Both in vivo and in vitro, Rbl2p forms a complex with beta-tubulin that does not contain alpha-tubulin, thus defining a second pool of beta-tubulin in the cell. Formation of the complex depends upon the conformation of beta-tubulin. Newly synthesized beta-tubulin can bind to Rbl2p before it binds to alpha-tubulin. Rbl2p can also bind beta-tubulin from the alpha/beta-tubulin heterodimer, apparently by competing with alpha-tubulin. The Rbl2p-beta-tubulin complex has a half-life of approximately 2.5 h and is less stable than the alpha/beta-tubulin heterodimer. The results of our experiments explain both how excess Rbl2p can rescue cells overexpressing beta-tubulin and how it can be deleterious in a wild-type background. They also suggest that the Rbl2p-beta-tubulin complex is part of a cellular mechanism for regulating the levels and dimerization of tubulin chains.
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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.