Knock Down of Heat Shock Protein 27 (HspB1) Induces Degradation of Several Putative Client Proteins

Autor: Maryline Moulin, Carole Kretz-Remy, Vincent Gonin, André-Patrick Arrigo, Frantz Bouhallier, Benjamin Gibert, Stéphanie Simon, Lydie Fasquelle, Benedicte Eckel, Chantal Diaz-Latoud, Gregory Mellier
Přispěvatelé: LATTEXLaboratorio de Tectonofisica e tectonica experimental, Universidade de Lisboa (ULISBOA), Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Institut de Génomique Fonctionnelle de Lyon (IGFL), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon), Comite du Rhone of la Ligue Contre le Cancer, Rhone-Alpes, École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Universidade de Lisboa = University of Lisbon (ULISBOA), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL)
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Proteomics
AKT activation
HSP27 Heat-Shock Proteins
lcsh:Medicine
Apoptosis
HSP27
Biochemistry
0302 clinical medicine
MESH: RNA
Small Interfering
Molecular Cell Biology
Macromolecular Structure Analysis
Tumor Cells
Cultured
MESH: Proteins
RNA
Small Interfering
lcsh:Science
Heat-Shock Proteins
Inhibition
Regulation of gene expression
0303 health sciences
Multidisciplinary
Prostate cancer
Physics
Transfection
MESH: Gene Expression Regulation
Neoplastic
Induced Apoptosis
Cell-death
Cytochrome-C
Androgen ablation
Deacetylase HDAC6
Tumor cells
Cell biology
Gene Expression Regulation
Neoplastic
MESH: Cell Survival
030220 oncology & carcinogenesis
Gene Knockdown Techniques
embryonic structures
MESH: Molecular Chaperones
Research Article
Protein Binding
endocrine system
animal structures
Cell Survival
Biophysics
MESH: Proteolysis
Biology
03 medical and health sciences
Hsp27
Heat shock protein
MESH: Protein Binding
Humans
MESH: Tumor Cells
Cultured
MESH: HSP27 Heat-Shock Proteins
Transcription factor
030304 developmental biology
MESH: Humans
MESH: Apoptosis
MESH: Transfection
lcsh:R
Proteins
Computational Biology
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
HDAC6
MESH: Gene Knockdown Techniques
Chaperone (protein)
MESH: HeLa Cells
Proteolysis
biology.protein
lcsh:Q
Histone deacetylase
HeLa Cells
Molecular Chaperones
Zdroj: PLoS ONE
PLoS ONE, Public Library of Science, 2012, 7 (1), pp.e29719. ⟨10.1371/journal.pone.0029719⟩
Plos One 1 (7), . (2012)
PLoS ONE, 2012, 7 (1), pp.e29719. ⟨10.1371/journal.pone.0029719⟩
PLoS ONE, Vol 7, Iss 1, p e29719 (2012)
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0029719⟩
Popis: International audience; Hsp27 belongs to the heat shock protein family and displays chaperone properties in stress conditions by holding unfolded polypeptides, hence avoiding their inclination to aggregate. Hsp27 is often referenced as an anti-cancer therapeutic target, but apart from its well-described ability to interfere with different stresses and apoptotic processes, its role in non-stressed conditions is still not well defined. In the present study we report that three polypeptides (histone deacetylase HDAC6, transcription factor STAT2 and procaspase-3) were degraded in human cancerous cells displaying genetically decreased levels of Hsp27. In addition, these proteins interacted with Hsp27 complexes of different native size. Altogether, these findings suggest that HDAC6, STAT2 and procaspase-3 are client proteins of Hsp27. Hence, in non stressed cancerous cells, the structural organization of Hsp27 appears to be a key parameter in the regulation by this chaperone of the level of specific polypeptides through client-chaperone type of interactions.
Databáze: OpenAIRE
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