Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes.

Cuesta, R; Laroia, G; Schneider, R J

Cuesta, R; Laroia, G; Schneider, R J.

Affiliation

Cuesta R; Department of Microbiology, New York University School of Medicine and Kaplan Cancer Center, New York, New York 10016 USA.

Genes Dev ; 14(12): 1460-70, 2000 Jun 15.

Article in En | MEDLINE | ID: mdl-10859165

Subject(s)

HSP70 Heat-Shock Proteins; Heat-Shock Proteins; Molecular Chaperones/physiology; Neoplasm Proteins/metabolism; Neoplasm Proteins/physiology; Peptide Initiation Factors/metabolism; Protein Biosynthesis; Animals; Blotting, Western; Carrier Proteins/metabolism; Cell Line, Transformed; Dose-Response Relationship, Drug; Eukaryotic Initiation Factor-4F; Eukaryotic Initiation Factor-4G; Fluorescent Antibody Technique; Glutathione Transferase/metabolism; HSC70 Heat-Shock Proteins; HSP27 Heat-Shock Proteins; HeLa Cells; Hot Temperature; Humans; Intracellular Signaling Peptides and Proteins; Mice; Molecular Chaperones/metabolism; Phosphotransferases/metabolism; Plasmids; Precipitin Tests; Protein Binding; Protein Serine-Threonine Kinases/metabolism; RNA Caps; RNA, Messenger/metabolism; Temperature; Transfection

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Biosynthesis / Peptide Initiation Factors / Molecular Chaperones / HSP70 Heat-Shock Proteins / Heat-Shock Proteins / Neoplasm Proteins Limits: Animals / Humans Language: En Journal: Genes Dev Journal subject: BIOLOGIA MOLECULAR Year: 2000 Document type: Article

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