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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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
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Abstract	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 induce Hsp90 acetylation and inhibit its activity. However, direct determination of the functional consequences of Hsp90 acetylation has awaited mapping of specific sites. We now demonstrate that Hsp90 K294 is acetylated. Mutational analysis of K294 shows that its acetylation status is a strong determinant of client protein and cochaperone binding. In yeast, Hsp90 mutants that cannot be acetylated at K294 have reduced viability and chaperone function compared to WT or to mutants that mimic constitutive acetylation. These data suggest that acetylation/deacetylation of K294 plays an important role in regulating the Hsp90 chaperone cycle.
AbstractList	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 induce Hsp90 acetylation and inhibit its activity. However, direct determination of the functional consequences of Hsp90 acetylation has awaited mapping of specific sites. We now demonstrate that Hsp90 K294 is acetylated. Mutational analysis of K294 shows that its acetylation status is a strong determinant of client protein and cochaperone binding. In yeast, Hsp90 mutants that cannot be acetylated at K294 have reduced viability and chaperone function compared to WT or to mutants that mimic constitutive acetylation. These data suggest that acetylation/deacetylation of K294 plays an important role in regulating the Hsp90 chaperone cycle.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 induce Hsp90 acetylation and inhibit its activity. However, direct determination of the functional consequences of Hsp90 acetylation has awaited mapping of specific sites. We now demonstrate that Hsp90 K294 is acetylated. Mutational analysis of K294 shows that its acetylation status is a strong determinant of client protein and cochaperone binding. In yeast, Hsp90 mutants that cannot be acetylated at K294 have reduced viability and chaperone function compared to WT or to mutants that mimic constitutive acetylation. These data suggest that acetylation/deacetylation of K294 plays an important role in regulating the Hsp90 chaperone cycle. 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 induce Hsp90 acetylation and inhibit its activity. However, direct determination of the functional consequences of Hsp90 acetylation has awaited mapping of specific sites. We now demonstrate that Hsp90 K294 is acetylated. Mutational analysis of K294 shows that its acetylation status is a strong determinant of client protein and cochaperone binding. In yeast, Hsp90 mutants that cannot be acetylated at K294 have reduced viability and chaperone function compared to WT or to mutants that mimic constitutive acetylation. These data suggest that acetylation/deacetylation of K294 plays an important role in regulating the Hsp90 chaperone cycle.
Author	Robzyk, Kenneth Beebe, Kristin Scroggins, Bradley T Tsutsumi, Shinji Wang, Dongxia Cotter, Robert J Marcu, Monica G Felts, Sara Karnitz, Larry Neckers, Len Rosen, Neal Toft, David
Author_xml	– sequence: 1 givenname: Bradley T surname: Scroggins fullname: Scroggins, Bradley T organization: Urologic Oncology Branch, National Cancer Institute, Bethesda, MD 20892, USA – sequence: 2 givenname: Kenneth surname: Robzyk fullname: Robzyk, Kenneth – sequence: 3 givenname: Dongxia surname: Wang fullname: Wang, Dongxia – sequence: 4 givenname: Monica G surname: Marcu fullname: Marcu, Monica G – sequence: 5 givenname: Shinji surname: Tsutsumi fullname: Tsutsumi, Shinji – sequence: 6 givenname: Kristin surname: Beebe fullname: Beebe, Kristin – sequence: 7 givenname: Robert J surname: Cotter fullname: Cotter, Robert J – sequence: 8 givenname: Sara surname: Felts fullname: Felts, Sara – sequence: 9 givenname: David surname: Toft fullname: Toft, David – sequence: 10 givenname: Larry surname: Karnitz fullname: Karnitz, Larry – sequence: 11 givenname: Neal surname: Rosen fullname: Rosen, Neal – sequence: 12 givenname: Len surname: Neckers fullname: Neckers, Len
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/17218278$$D View this record in MEDLINE/PubMed
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Snippet	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...
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SubjectTerms	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
Title	An acetylation site in the middle domain of Hsp90 regulates chaperone function
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