ArticlePloS one2010
Mutation of Ser172 in yeast β tubulin induces defects in microtubule dynamics and cell division.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- How phosphorylation of α/β-tubulin perturbs microtubule structure: A computational study.The Journal of biological chemistry · 2026Article
- Deciphering the tubulin code: roles and mechanisms of microtubule post-translational modifications in gastrointestinal tumors: a narrative review.Journal of gastrointestinal oncology · 2026Review
- Phospho-mimic βIII-tubulin rescues microtubule and cardiac defects in Duchenne muscular dystrophy mice.Journal of molecular and cellular cardiology · 2026Article
- Emerging Roles of Tubulin Isoforms and Their Post-Translational Modifications in Microtubule-Based Transport and Cellular Functions.Biomolecules · 2026Review
- PP2A phosphatase regulates cell-type specific cytoskeletal organization to drive dendrite diversity.Frontiers in molecular neuroscience · 2022Article
- Tubulin post-translational modifications control neuronal development and functions.Developmental neurobiology · 2021Review
- Systematic Humanization of the Yeast Cytoskeleton Discerns Functionally Replaceable from Divergent Human Genes.Genetics · 2020Article
- The tubulin code and its role in controlling microtubule properties and functions.Nature reviews. Molecular cell biology · 2020Review
- Tubulin Post-Translational Modifications and Microtubule Dynamics.International journal of molecular sciences · 2017Review
- The Tubulin Code: A Navigation System for Chromosomes during Mitosis.Trends in cell biology · 2016Review
- The tubulin code: molecular components, readout mechanisms, and functions.The Journal of cell biology · 2014Review
- Adhesion of Trypanosoma cruzi trypomastigotes to fibronectin or laminin modifies tubulin and paraflagellar rod protein phosphorylation.PloS one · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ser172 of β tubulin is an important residue that is mutated in a human brain disease and phosphorylated by the cyclin-dependent kinase Cdk1 in mammalian cells. To examine the role of this residue, we used the yeast S. cerevisiae as a model and produced two different mutations (S172A and S172E) of the conserved Ser172 in the yeast β tubulin Tub2p. The two mutants showed impaired cell growth on benomyl-containing medium and at cold temperatures, altered microtubule (MT) dynamics, and altered nucleus positioning and segregation. When cytoplasmic MT effectors Dyn1p or Kar9p were deleted in S172A and S172E mutants, cells were viable but presented increased ploidy. Furthermore, the two β tubulin mutations exhibited synthetic lethal interactions with Bik1p, Bim1p or Kar3p, which are effectors of cytoplasmic and spindle MTs. In the absence of Mad2p-dependent spindle checkpoint, both mutations are deleterious. These findings show the importance of Ser172 for the correct function of both cytoplasmic and spindle MTs and for normal cell division.
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