Stathmin: A Tubulin-Sequestering Protein Which Forms a Ternary T2S Complex with Two Tubulin Molecules
Abstract
Stathmin is an important regulatory protein thought to control the dynamics of microtubules through the cell cycle in a phosphorylation-dependent manner. Here we show that stathmin interacts with two molecules of dimeric alphabeta-tubulin to form a tight ternary T2S complex, sedimenting at 7.7 S. This complex appears in slow association-dissociation equilibrium in the analytical ultracentrifuge. The T2S complex is formed under a variety of ionic conditions, either from GTP- or GDP-tubulin or from the tubulin-colchicine complex. The S16/25/38/63E mutated stathmin in contrast is in rapid equilibrium with tubulin in the T2S complex. The T2S complex cannot polymerize in microtubules nor in ring oligomers. Stathmin acts as a pure tubulin-sequestering protein via formation of the T2S complex. It does not act directly on microtubule ends to promote catastrophe nor enhance microtubule dynamics.
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Non-phosphorylated stathmin 1 can associate with α/β tubulin subunits to induce microtubule destabilization.
“While the effect of stathmin 1K9Ac on MAPK pathways has not yet been elucidated, non-phosphorylated stathmin 1 can associate with α/β tubulin subunits to induce microtubule destabilization [95].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [95]
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Probing the Native Structure of Stathmin and Its Interaction Domains with Tubulin
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Prion protein inhibits microtubule assembly by inducing tubulin oligomerization
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Microtubule destruction induces tau liberation and its subsequent phosphorylation
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- Authors
- Jourdain, L., Curmi, P., Sobel, A., Pantaloni, D., & Carlier, M.-F.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Carlier, Marie-France
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1997-09-01
- Volume
- 36
- Issue
- 36
- Pages
- 10817-10821
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2003878410
- Cited by
- 245
- References
- 12
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 3 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 6 · 2018: 4 · 2017: 7 · 2016: 5 · 2015: 7 · 2014: 13 · 2013: 12 · 2012: 9
- FWCI
- 5.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Physical Sciences › Chemistry › Organic Chemistry › Synthesis and biological activity
- Keywords
- stathmin, microtubule dynamics, tubulin phosphorylation, colchicine, microtubule assembly
- MeSH terms
- Animals, Microtubule Proteins, Microtubules, Phosphoproteins, Protein Binding, Tubulin, Ultracentrifugation, Dimerization, Stathmin
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