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; pp. 151 - 159 |
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| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
12.01.2007
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1097-2765 1097-4164 |
| DOI | 10.1016/j.molcel.2006.12.008 |
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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. |
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| 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 post-translational modifications which affect its function, including acetylation. Histone deacetylase (HDAC) inhibitors and knock-down 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 wild type 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 Tsutsumi, Shinji Wang, Dongxia Felts, Sara Karnitz, Larry Neckers, Len Marcu, Monica G. Scroggins, Bradley T. Cotter, Robert J. 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 organization: Department of Medicine and Program in Cell Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA – sequence: 3 givenname: Dongxia surname: Wang fullname: Wang, Dongxia organization: Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA – sequence: 4 givenname: Monica G. surname: Marcu fullname: Marcu, Monica G. organization: Urologic Oncology Branch, National Cancer Institute, Bethesda, MD 20892, USA – sequence: 5 givenname: Shinji surname: Tsutsumi fullname: Tsutsumi, Shinji organization: Urologic Oncology Branch, National Cancer Institute, Bethesda, MD 20892, USA – sequence: 6 givenname: Kristin surname: Beebe fullname: Beebe, Kristin organization: Urologic Oncology Branch, National Cancer Institute, Bethesda, MD 20892, USA – sequence: 7 givenname: Robert J. surname: Cotter fullname: Cotter, Robert J. organization: Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA – sequence: 8 givenname: Sara surname: Felts fullname: Felts, Sara organization: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA – sequence: 9 givenname: David surname: Toft fullname: Toft, David organization: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA – sequence: 10 givenname: Larry surname: Karnitz fullname: Karnitz, Larry organization: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA – sequence: 11 givenname: Neal surname: Rosen fullname: Rosen, Neal organization: Department of Medicine and Program in Cell Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA – sequence: 12 givenname: Len surname: Neckers fullname: Neckers, Len email: len@helix.nih.gov organization: Urologic Oncology Branch, National Cancer Institute, Bethesda, MD 20892, USA |
| 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... 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 PROTEINS Saccharomyces cerevisiae - cytology |
| Title | An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function |
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