Human Fas-associated Factor 1 Interacts with Heat Shock Protein 70 and Negatively Regulates Chaperone Activity
We examined the cell death-inducing property of human Fas-associated factor 1 (hFAF1) in the heat shock signaling pathway. By employing co-immunoprecipitation and peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight mass spectrometry, we found that hFAF1 binds...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-03, Vol.280 (9), p.8125-8133 |
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| container_title | The Journal of biological chemistry |
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| creator | Kim, Hee-Jung Song, Eun Joo Lee, Yun-Suk Kim, Eunhee Lee, Kong-Joo |
| description | We examined the cell death-inducing property of human Fas-associated factor 1 (hFAF1) in the heat shock signaling pathway.
By employing co-immunoprecipitation and peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight
mass spectrometry, we found that hFAF1 binds to the 70-kDa heat shock protein family (Hsc70/Hsp70). Interaction mapping indicated
that the 82â180 sequence of hFAF1 directly binds to the N-terminal region containing sequence 1â120 of Hsc70/Hsp70. This binding
is very tight regardless of ATP and heat shock treatment. Hsc70/Hsp70 and hFAF1 co-localized in the cytosol and nucleus and
concentrated to the perinuclear region by heat shock treatment. We examined how hFAF1 regulates Hsp70 function, and found
that hFAF1 inhibited the Hsp70 chaperone activity of refolding denatured protein substrates, accelerated heat shock-induced
SAPK/JNK activation, and raised heat shock-induced cell death in a binding dependent manner. These results suggest that hFAF1
prevents cells from recovery after stress by binding to and inhibiting the chaperone activity of Hsp70. |
| doi_str_mv | 10.1074/jbc.M406297200 |
| format | Article |
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By employing co-immunoprecipitation and peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight
mass spectrometry, we found that hFAF1 binds to the 70-kDa heat shock protein family (Hsc70/Hsp70). Interaction mapping indicated
that the 82â180 sequence of hFAF1 directly binds to the N-terminal region containing sequence 1â120 of Hsc70/Hsp70. This binding
is very tight regardless of ATP and heat shock treatment. Hsc70/Hsp70 and hFAF1 co-localized in the cytosol and nucleus and
concentrated to the perinuclear region by heat shock treatment. We examined how hFAF1 regulates Hsp70 function, and found
that hFAF1 inhibited the Hsp70 chaperone activity of refolding denatured protein substrates, accelerated heat shock-induced
SAPK/JNK activation, and raised heat shock-induced cell death in a binding dependent manner. These results suggest that hFAF1
prevents cells from recovery after stress by binding to and inhibiting the chaperone activity of Hsp70.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M406297200</identifier><identifier>PMID: 15596450</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adaptor Proteins, Signal Transducing ; Adenosine Triphosphate - chemistry ; Apoptosis Regulatory Proteins ; Carrier Proteins - metabolism ; Cell Line ; Cell Nucleus - metabolism ; Cytosol - metabolism ; Electrophoresis, Gel, Two-Dimensional ; Gene Expression Regulation ; Glutathione Transferase - metabolism ; Heat-Shock Proteins - metabolism ; HeLa Cells ; HSC70 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins - chemistry ; HSP70 Heat-Shock Proteins - metabolism ; Humans ; Immunoprecipitation ; Luciferases - metabolism ; Mass Spectrometry ; Microscopy, Confocal ; Microscopy, Fluorescence ; Mitogen-Activated Protein Kinase 8 - metabolism ; Models, Genetic ; Molecular Chaperones - metabolism ; Plasmids - metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Time Factors ; Transfection</subject><ispartof>The Journal of biological chemistry, 2005-03, Vol.280 (9), p.8125-8133</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-c3e41e946aa7d9d54da8f05e121999c4f1dc298a951aa58fc4a954152fcb407d3</citedby><cites>FETCH-LOGICAL-c360t-c3e41e946aa7d9d54da8f05e121999c4f1dc298a951aa58fc4a954152fcb407d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15596450$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Hee-Jung</creatorcontrib><creatorcontrib>Song, Eun Joo</creatorcontrib><creatorcontrib>Lee, Yun-Suk</creatorcontrib><creatorcontrib>Kim, Eunhee</creatorcontrib><creatorcontrib>Lee, Kong-Joo</creatorcontrib><title>Human Fas-associated Factor 1 Interacts with Heat Shock Protein 70 and Negatively Regulates Chaperone Activity</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We examined the cell death-inducing property of human Fas-associated factor 1 (hFAF1) in the heat shock signaling pathway.
By employing co-immunoprecipitation and peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight
mass spectrometry, we found that hFAF1 binds to the 70-kDa heat shock protein family (Hsc70/Hsp70). Interaction mapping indicated
that the 82â180 sequence of hFAF1 directly binds to the N-terminal region containing sequence 1â120 of Hsc70/Hsp70. This binding
is very tight regardless of ATP and heat shock treatment. Hsc70/Hsp70 and hFAF1 co-localized in the cytosol and nucleus and
concentrated to the perinuclear region by heat shock treatment. We examined how hFAF1 regulates Hsp70 function, and found
that hFAF1 inhibited the Hsp70 chaperone activity of refolding denatured protein substrates, accelerated heat shock-induced
SAPK/JNK activation, and raised heat shock-induced cell death in a binding dependent manner. These results suggest that hFAF1
prevents cells from recovery after stress by binding to and inhibiting the chaperone activity of Hsp70.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>Apoptosis Regulatory Proteins</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cell Nucleus - metabolism</subject><subject>Cytosol - metabolism</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Gene Expression Regulation</subject><subject>Glutathione Transferase - metabolism</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>HeLa Cells</subject><subject>HSC70 Heat-Shock Proteins</subject><subject>HSP70 Heat-Shock Proteins - chemistry</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Luciferases - metabolism</subject><subject>Mass Spectrometry</subject><subject>Microscopy, Confocal</subject><subject>Microscopy, Fluorescence</subject><subject>Mitogen-Activated Protein Kinase 8 - metabolism</subject><subject>Models, Genetic</subject><subject>Molecular Chaperones - metabolism</subject><subject>Plasmids - metabolism</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary</subject><subject>Signal Transduction</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Time Factors</subject><subject>Transfection</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM1P3DAQxa2Kqiy01x4ri0Nv2dqOncRHtAIWCWjVD6k3a9aZbEyTeLGdov3vMdqVmMPMPM1v3uER8pmzJWe1_Pa4sct7ySqha8HYO7LgrCmLUvG_J2TBmOCFFqo5JWcxPrJcUvMP5JQrpSup2IJM63mEiV5DLCBGbx0kbLO0yQfK6e2UMGQR6bNLPV0jJPqr9_Yf_RF8QjfRmlGYWvqAW0juPw57-hO385BtIl31sMPgJ6SXNh9d2n8k7zsYIn46znPy5_rq92pd3H2_uV1d3hW2rFjKHSVHLSuAutWtki00HVPIBddaW9nx1grdgFYcQDWdlXmVXInObiSr2_KcfD347oJ_mjEmM7pocRhgQj9HU9WyqmrOMrg8gDb4GAN2ZhfcCGFvODOvCZucsHlLOD98OTrPmxHbN_wYaQYuDkDvtv2zC2g2ztseRyMaZrRpuFDlC3UEgpY</recordid><startdate>20050304</startdate><enddate>20050304</enddate><creator>Kim, Hee-Jung</creator><creator>Song, Eun Joo</creator><creator>Lee, Yun-Suk</creator><creator>Kim, Eunhee</creator><creator>Lee, Kong-Joo</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20050304</creationdate><title>Human Fas-associated Factor 1 Interacts with Heat Shock Protein 70 and Negatively Regulates Chaperone Activity</title><author>Kim, Hee-Jung ; Song, Eun Joo ; Lee, Yun-Suk ; Kim, Eunhee ; Lee, Kong-Joo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-c3e41e946aa7d9d54da8f05e121999c4f1dc298a951aa58fc4a954152fcb407d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>Apoptosis Regulatory Proteins</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cell Nucleus - metabolism</topic><topic>Cytosol - metabolism</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Gene Expression Regulation</topic><topic>Glutathione Transferase - metabolism</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>HeLa Cells</topic><topic>HSC70 Heat-Shock Proteins</topic><topic>HSP70 Heat-Shock Proteins - chemistry</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Luciferases - metabolism</topic><topic>Mass Spectrometry</topic><topic>Microscopy, Confocal</topic><topic>Microscopy, Fluorescence</topic><topic>Mitogen-Activated Protein Kinase 8 - metabolism</topic><topic>Models, Genetic</topic><topic>Molecular Chaperones - metabolism</topic><topic>Plasmids - metabolism</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>Signal Transduction</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Time Factors</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Hee-Jung</creatorcontrib><creatorcontrib>Song, Eun Joo</creatorcontrib><creatorcontrib>Lee, Yun-Suk</creatorcontrib><creatorcontrib>Kim, Eunhee</creatorcontrib><creatorcontrib>Lee, Kong-Joo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Hee-Jung</au><au>Song, Eun Joo</au><au>Lee, Yun-Suk</au><au>Kim, Eunhee</au><au>Lee, Kong-Joo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Fas-associated Factor 1 Interacts with Heat Shock Protein 70 and Negatively Regulates Chaperone Activity</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-03-04</date><risdate>2005</risdate><volume>280</volume><issue>9</issue><spage>8125</spage><epage>8133</epage><pages>8125-8133</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>We examined the cell death-inducing property of human Fas-associated factor 1 (hFAF1) in the heat shock signaling pathway.
By employing co-immunoprecipitation and peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight
mass spectrometry, we found that hFAF1 binds to the 70-kDa heat shock protein family (Hsc70/Hsp70). Interaction mapping indicated
that the 82â180 sequence of hFAF1 directly binds to the N-terminal region containing sequence 1â120 of Hsc70/Hsp70. This binding
is very tight regardless of ATP and heat shock treatment. Hsc70/Hsp70 and hFAF1 co-localized in the cytosol and nucleus and
concentrated to the perinuclear region by heat shock treatment. We examined how hFAF1 regulates Hsp70 function, and found
that hFAF1 inhibited the Hsp70 chaperone activity of refolding denatured protein substrates, accelerated heat shock-induced
SAPK/JNK activation, and raised heat shock-induced cell death in a binding dependent manner. These results suggest that hFAF1
prevents cells from recovery after stress by binding to and inhibiting the chaperone activity of Hsp70.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15596450</pmid><doi>10.1074/jbc.M406297200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Adenosine Triphosphate - chemistry Apoptosis Regulatory Proteins Carrier Proteins - metabolism Cell Line Cell Nucleus - metabolism Cytosol - metabolism Electrophoresis, Gel, Two-Dimensional Gene Expression Regulation Glutathione Transferase - metabolism Heat-Shock Proteins - metabolism HeLa Cells HSC70 Heat-Shock Proteins HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - metabolism Humans Immunoprecipitation Luciferases - metabolism Mass Spectrometry Microscopy, Confocal Microscopy, Fluorescence Mitogen-Activated Protein Kinase 8 - metabolism Models, Genetic Molecular Chaperones - metabolism Plasmids - metabolism Protein Binding Protein Folding Protein Structure, Tertiary Signal Transduction Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Time Factors Transfection |
| title | Human Fas-associated Factor 1 Interacts with Heat Shock Protein 70 and Negatively Regulates Chaperone Activity |
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