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Loss of α-Tubulin Acetylation Is Associated with TGF-β-induced Epithelial-Mesenchymal Transition
- Source :
- Journal of Biological Chemistry. 291:5396-5405
- Publication Year :
- 2016
- Publisher :
- Elsevier BV, 2016.
-
Abstract
- The epithelial-to-mesenchymal transition (EMT) is a process by which differentiated epithelial cells reprogram gene expression, lose their junctions and polarity, reorganize their cytoskeleton, increase cell motility and assume a mesenchymal morphology. Despite the critical functions of the microtubule (MT) in cytoskeletal organization, how it participates in EMT induction and maintenance remains poorly understood. Here we report that acetylated α-tubulin, which plays an important role in microtubule (MT) stabilization and cell morphology, can serve as a novel regulator and marker of EMT. A high level of acetylated α-tubulin was correlated with epithelial morphology and it profoundly decreased during TGF-β-induced EMT. We found that TGF-β increased the activity of HDAC6, a major deacetylase of α-tubulin, without affecting its expression levels. Treatment with HDAC6 inhibitor tubacin or TGF-β type I receptor inhibitor SB431542 restored the level of acetylated α-tubulin and consequently blocked EMT. Our results demonstrate that acetylated α-tubulin can serve as a marker of EMT and that HDAC6 represents an important regulator during EMT process.
- Subjects :
- 0301 basic medicine
Epithelial-Mesenchymal Transition
Dioxoles
Biology
Histone Deacetylase 6
Hydroxamic Acids
Cell morphology
Microtubules
Biochemistry
Histone Deacetylases
Mice
03 medical and health sciences
Transforming Growth Factor beta
Tubulin
Microtubule
Animals
Humans
Anilides
Epithelial–mesenchymal transition
Cytoskeleton
Molecular Biology
Acetylation
Cell Biology
Transforming growth factor beta
HDAC6
Cell biology
HEK293 Cells
030104 developmental biology
Benzamides
embryonic structures
MCF-7 Cells
biology.protein
Protein Processing, Post-Translational
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 291
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....22a659ef123fbe7e2a58d891051cd556