Journal
CELLULAR SIGNALLING
Volume 21, Issue 4, Pages 529-539Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2008.12.004
Keywords
Hsp90; Microtubule; Acetylation; Akt; p53
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Funding
- Ministere de I'Enseignement Superieur et de la Recherche [UPRES JE2493]
- Institut de Recherche Internationale Servier (France)
- Ligue Nationale contre le Cancer
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Involved in a wide range of cellular processes such as signal transduction, microtubules are highly dynamic polymers that accumulate various post-translational modifications including polyglutamylation, polyglycylation, carboxyterminal cleavage and acetylation, the functions of which just begin to be uncovered. The molecular chaperone Hsp90, which is essential for the folding and activity of numerous client proteins involved in cell proliferation and apoptosis, associates with the microtubule network but the effects of tubulin post-translational modifications on its microtubule binding has not yet been investigated. Herein, we show that both the constitutive (beta) and the inducible (alpha) Hsp90 isoforms bind to microtubules in a way that depends on the level of tubulin acetylation. Tubulin acetylation also stimulates the binding and the signaling function of at least two of its client proteins, the kinase Akt/PKB and the transcription factor p53. This study highlights the role of tubulin acetylation in modulating microtubule-based transport of Hsp90-chaperoned proteins and thus in regulating signaling dynamics in the cytoplasm. (C) 2008 Elsevier Inc. All rights reserved.
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