An acetylation site in the middle domain of Hsp90 regulates chaperone function

Heat-shock protein 90 (Hsp90) chaperones a key subset of signaling proteins and is necessary for malignant transformation. Hsp90 is subject to an array of posttranslational modifications that affect its function, including acetylation. Histone deacetylase (HDAC) inhibitors and knockdown of HDAC6 ind...

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Bibliographic Details
Published in:	Molecular cell Vol. 25; no. 1; p. 151
Main Authors:	Scroggins, Bradley T, Robzyk, Kenneth, Wang, Dongxia, Marcu, Monica G, Tsutsumi, Shinji, Beebe, Kristin, Cotter, Robert J, Felts, Sara, Toft, David, Karnitz, Larry, Rosen, Neal, Neckers, Len
Format:	Journal Article
Language:	English
Published:	United States 12.01.2007
Subjects:	Acetylation Amino Acid Sequence Animals Cercopithecus aethiops Checkpoint Kinase 1 COS Cells HSP90 Heat-Shock Proteins - chemistry HSP90 Heat-Shock Proteins - metabolism Humans Lysine - metabolism Mice Molecular Sequence Data Mutant Proteins - chemistry Mutant Proteins - metabolism Mutation - genetics NIH 3T3 Cells Protein Binding Protein Kinases - metabolism Protein Structure, Tertiary Saccharomyces cerevisiae - cytology
ISSN:	1097-2765
Online Access:	Get more information
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