ArticleThe Journal of biological chemistry2010
Drosophila stathmins bind tubulin heterodimers with high and variable stoichiometries.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Shared candidate genes associated with variation in egg size in cold-adapted and artificially selected Drosophila melanogaster.Developmental biology · 2026Article
- Microtubules, Membranes, and Movement: New Roles for Stathmin-2 in Axon Integrity.Journal of neuroscience research · 2024Review
- The disease-associated proteins Drosophila Nab2 and Ataxin-2 interact with shared RNAs and coregulate neuronal morphology.Genetics · 2022Article
- Mask, the Drosophila ankyrin repeat and KH domain-containing protein, affects microtubule stability.Journal of cell science · 2021Article
- Comparative proteomes change and possible role in different pathways of microRNA-21a-5p in a mouse model of spinal cord injury.Neural regeneration research · 2020Article
- Developmental arrest ofDevelopment (Cambridge, England) · 2020Article
- Stathmin overexpression is associated with growth, invasion and metastasis of lung adenocarcinoma.Oncotarget · 2017Article
- Stathmin-dependent molecular targeting therapy for malignant tumor: the latest 5 years' discoveries and developments.Journal of translational medicine · 2016Review
- A conceptual view at microtubule plus end dynamics in neuronal axons.Brain research bulletin · 2016Review
- The Microtubule Regulatory Protein Stathmin Is Required to Maintain the Integrity of Axonal Microtubules in Drosophila.PloS one · 2013Article
- Design and characterization of modular scaffolds for tubulin assembly.The Journal of biological chemistry · 2012Article
- Specific serine-proline phosphorylation and glycogen synthase kinase 3β-directed subcellular targeting of stathmin 3/Sclip in neurons.The Journal of biological chemistry · 2012Article
- Stathmin is required for stability of the Drosophila neuromuscular junction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.The Journal of biological chemistry · 2011Article
- Subcellular Golgi localization of stathmin family proteins is promoted by a specific set of DHHC palmitoyl transferases.Molecular biology of the cell · 2011Article
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In vertebrates, stathmins form a family of proteins possessing two tubulin binding repeats (TBRs), which each binds one soluble tubulin heterodimer. The stathmins thus sequester two tubulins in a phosphorylation-dependent manner, providing a link between signal transduction and microtubule dynamics. In Drosophila, we show here that a single stathmin gene (stai) encodes a family of D-stathmin proteins. Two of the D-stathmins are maternally deposited and then restricted to germ cells, and the other two are detected in the nervous system during embryo development. Like in vertebrates, the nervous system-enriched stathmins contain an N-terminal domain involved in subcellular targeting. All the D-stathmins possess a domain containing three or four predicted TBRs, and we demonstrate here, using complementary biochemical and biophysical methods, that all four predicted TBR domains actually bind tubulin. D-stathmins can indeed bind up to four tubulins, the resulting complex being directly visualized by electron microscopy. Phylogenetic analysis shows that the presence of regulated multiple tubulin sites is a conserved characteristic of stathmins in invertebrates and allows us to predict key residues in stathmin for the binding of tubulin. Altogether, our results reveal that the single Drosophila stathmin gene codes for a stathmin family similar to the multigene vertebrate one, but with particular tubulin binding properties.
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