Analysis of the subcellular localization of the human histone methyltransferase SETDB1
SET domain, bifurcated 1 (SETDB1) is a histone methyltransferase that methylates lysine 9 on histone H3. Although it is important to know the localization of proteins to elucidate their physiological function, little is known of the subcellular localization of human SETDB1. In the present study, to...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2015-10, Vol.465 (4), p.725-731 |
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| creator | Tachibana, Keisuke Gotoh, Eiko Kawamata, Natsuko Ishimoto, Kenji Uchihara, Yoshie Iwanari, Hiroko Sugiyama, Akira Kawamura, Takeshi Mochizuki, Yasuhiro Tanaka, Toshiya Sakai, Juro Hamakubo, Takao Kodama, Tatsuhiko Doi, Takefumi |
| description | SET domain, bifurcated 1 (SETDB1) is a histone methyltransferase that methylates lysine 9 on histone H3. Although it is important to know the localization of proteins to elucidate their physiological function, little is known of the subcellular localization of human SETDB1. In the present study, to investigate the subcellular localization of hSETDB1, we established a human cell line constitutively expressing enhanced green fluorescent protein fused to hSETDB1. We then generated a monoclonal antibody against the hSETDB1 protein. Expression of both exogenous and endogenous hSETDB1 was observed mainly in the cytoplasm of various human cell lines. Combined treatment with the nuclear export inhibitor leptomycin B and the proteasome inhibitor MG132 led to the accumulation of hSETDB1 in the nucleus. These findings suggest that hSETDB1, localized in the nucleus, might undergo degradation by the proteasome and be exported to the cytosol, resulting in its detection mainly in the cytosol.
•Endogenous human SETDB1 was localized mainly in the cytoplasm.•Combined treatment with LMB and MG132 led to accumulation of human SETDB1 in the nucleus.•HeLa cells expressing EFGP-hSETDB1 are useful for subcellular localization analyses. |
| doi_str_mv | 10.1016/j.bbrc.2015.08.065 |
| format | Article |
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•Endogenous human SETDB1 was localized mainly in the cytoplasm.•Combined treatment with LMB and MG132 led to accumulation of human SETDB1 in the nucleus.•HeLa cells expressing EFGP-hSETDB1 are useful for subcellular localization analyses.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2015.08.065</identifier><identifier>PMID: 26296461</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; Active Transport, Cell Nucleus - drug effects ; Amino Acid Sequence ; BUILDUP ; Cell Line ; CELL NUCLEI ; Cell Nucleus - metabolism ; CHROMOSOMES ; CYTOPLASM ; Cytoplasm - metabolism ; Exportin 1 Protein ; Fatty Acids, Unsaturated - pharmacology ; FLUORESCENCE ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; HEK293 Cells ; HELA CELLS ; Hep G2 Cells ; Histone methyltransferase ; Histone-Lysine N-Methyltransferase ; HISTONES ; HUMAN POPULATIONS ; Humans ; Karyopherins - antagonists & inhibitors ; Leupeptins - pharmacology ; LYSINE ; METHYL TRANSFERASES ; Molecular Sequence Data ; MONOCLONAL ANTIBODIES ; Monoclonal antibody ; Proteasome Endopeptidase Complex - metabolism ; Proteasome Inhibitors - pharmacology ; Protein localization ; Protein Methyltransferases - genetics ; Protein Methyltransferases - metabolism ; Receptors, Cytoplasmic and Nuclear - antagonists & inhibitors ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Sequence Deletion ; SETDB1 ; Subcellular Fractions - metabolism</subject><ispartof>Biochemical and biophysical research communications, 2015-10, Vol.465 (4), p.725-731</ispartof><rights>2015 Elsevier Inc.</rights><rights>Copyright © 2015 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-7e2da3d1e96b144f904a899f3d0efbb3dac108c46123615f3e8628798842f2b83</citedby><cites>FETCH-LOGICAL-c520t-7e2da3d1e96b144f904a899f3d0efbb3dac108c46123615f3e8628798842f2b83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2015.08.065$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26296461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22592744$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Tachibana, Keisuke</creatorcontrib><creatorcontrib>Gotoh, Eiko</creatorcontrib><creatorcontrib>Kawamata, Natsuko</creatorcontrib><creatorcontrib>Ishimoto, Kenji</creatorcontrib><creatorcontrib>Uchihara, Yoshie</creatorcontrib><creatorcontrib>Iwanari, Hiroko</creatorcontrib><creatorcontrib>Sugiyama, Akira</creatorcontrib><creatorcontrib>Kawamura, Takeshi</creatorcontrib><creatorcontrib>Mochizuki, Yasuhiro</creatorcontrib><creatorcontrib>Tanaka, Toshiya</creatorcontrib><creatorcontrib>Sakai, Juro</creatorcontrib><creatorcontrib>Hamakubo, Takao</creatorcontrib><creatorcontrib>Kodama, Tatsuhiko</creatorcontrib><creatorcontrib>Doi, Takefumi</creatorcontrib><title>Analysis of the subcellular localization of the human histone methyltransferase SETDB1</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>SET domain, bifurcated 1 (SETDB1) is a histone methyltransferase that methylates lysine 9 on histone H3. Although it is important to know the localization of proteins to elucidate their physiological function, little is known of the subcellular localization of human SETDB1. In the present study, to investigate the subcellular localization of hSETDB1, we established a human cell line constitutively expressing enhanced green fluorescent protein fused to hSETDB1. We then generated a monoclonal antibody against the hSETDB1 protein. Expression of both exogenous and endogenous hSETDB1 was observed mainly in the cytoplasm of various human cell lines. Combined treatment with the nuclear export inhibitor leptomycin B and the proteasome inhibitor MG132 led to the accumulation of hSETDB1 in the nucleus. These findings suggest that hSETDB1, localized in the nucleus, might undergo degradation by the proteasome and be exported to the cytosol, resulting in its detection mainly in the cytosol.
•Endogenous human SETDB1 was localized mainly in the cytoplasm.•Combined treatment with LMB and MG132 led to accumulation of human SETDB1 in the nucleus.•HeLa cells expressing EFGP-hSETDB1 are useful for subcellular localization analyses.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Active Transport, Cell Nucleus - drug effects</subject><subject>Amino Acid Sequence</subject><subject>BUILDUP</subject><subject>Cell Line</subject><subject>CELL NUCLEI</subject><subject>Cell Nucleus - metabolism</subject><subject>CHROMOSOMES</subject><subject>CYTOPLASM</subject><subject>Cytoplasm - metabolism</subject><subject>Exportin 1 Protein</subject><subject>Fatty Acids, Unsaturated - pharmacology</subject><subject>FLUORESCENCE</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>HEK293 Cells</subject><subject>HELA CELLS</subject><subject>Hep G2 Cells</subject><subject>Histone methyltransferase</subject><subject>Histone-Lysine N-Methyltransferase</subject><subject>HISTONES</subject><subject>HUMAN POPULATIONS</subject><subject>Humans</subject><subject>Karyopherins - antagonists & inhibitors</subject><subject>Leupeptins - pharmacology</subject><subject>LYSINE</subject><subject>METHYL TRANSFERASES</subject><subject>Molecular Sequence Data</subject><subject>MONOCLONAL ANTIBODIES</subject><subject>Monoclonal antibody</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Proteasome Inhibitors - pharmacology</subject><subject>Protein localization</subject><subject>Protein Methyltransferases - genetics</subject><subject>Protein Methyltransferases - metabolism</subject><subject>Receptors, Cytoplasmic and Nuclear - antagonists & inhibitors</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Deletion</subject><subject>SETDB1</subject><subject>Subcellular Fractions - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAQx4Mouj6-gAcpeG6dpGk2AS--FQQPPvAW0nRCs3RbSbLC-ultWfXoaQ7zf8z8CDmmUFCg4mxR1HWwBQNaFSALENUWmVFQkDMKfJvMAEDkTNH3PbIf4wKAUi7ULtljginBBZ2Rt4vedOvoYza4LLWYxVVtsetWnQlZN1jT-S-T_ND_7tvV0vRZ62MaesyWmNp1l4Lpo8NgImbPNy_Xl_SQ7DjTRTz6mQfk9fbm5eo-f3y6e7i6eMxtxSDlc2SNKRuKStSUc6eAG6mUKxtAV9dlYywFacdLWSlo5UqUgsm5kpIzx2pZHpDTTe4Qk9fR-oS2tUPfo02asUqxOeejim1UNgwxBnT6I_ilCWtNQU8o9UJPKPWEUoPUI8rRdLIxfazqJTZ_ll92o-B8I8DxwU-PYerH3mLjw1TfDP6__G9N3YTB</recordid><startdate>20151002</startdate><enddate>20151002</enddate><creator>Tachibana, Keisuke</creator><creator>Gotoh, Eiko</creator><creator>Kawamata, Natsuko</creator><creator>Ishimoto, Kenji</creator><creator>Uchihara, Yoshie</creator><creator>Iwanari, Hiroko</creator><creator>Sugiyama, Akira</creator><creator>Kawamura, Takeshi</creator><creator>Mochizuki, Yasuhiro</creator><creator>Tanaka, Toshiya</creator><creator>Sakai, Juro</creator><creator>Hamakubo, Takao</creator><creator>Kodama, Tatsuhiko</creator><creator>Doi, Takefumi</creator><general>Elsevier Inc</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>OTOTI</scope></search><sort><creationdate>20151002</creationdate><title>Analysis of the subcellular localization of the human histone methyltransferase SETDB1</title><author>Tachibana, Keisuke ; Gotoh, Eiko ; Kawamata, Natsuko ; Ishimoto, Kenji ; Uchihara, Yoshie ; Iwanari, Hiroko ; Sugiyama, Akira ; Kawamura, Takeshi ; Mochizuki, Yasuhiro ; Tanaka, Toshiya ; Sakai, Juro ; Hamakubo, Takao ; Kodama, Tatsuhiko ; Doi, Takefumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c520t-7e2da3d1e96b144f904a899f3d0efbb3dac108c46123615f3e8628798842f2b83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Active Transport, Cell Nucleus - drug effects</topic><topic>Amino Acid Sequence</topic><topic>BUILDUP</topic><topic>Cell Line</topic><topic>CELL NUCLEI</topic><topic>Cell Nucleus - metabolism</topic><topic>CHROMOSOMES</topic><topic>CYTOPLASM</topic><topic>Cytoplasm - metabolism</topic><topic>Exportin 1 Protein</topic><topic>Fatty Acids, Unsaturated - pharmacology</topic><topic>FLUORESCENCE</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>HEK293 Cells</topic><topic>HELA CELLS</topic><topic>Hep G2 Cells</topic><topic>Histone methyltransferase</topic><topic>Histone-Lysine N-Methyltransferase</topic><topic>HISTONES</topic><topic>HUMAN POPULATIONS</topic><topic>Humans</topic><topic>Karyopherins - antagonists & inhibitors</topic><topic>Leupeptins - pharmacology</topic><topic>LYSINE</topic><topic>METHYL TRANSFERASES</topic><topic>Molecular Sequence Data</topic><topic>MONOCLONAL ANTIBODIES</topic><topic>Monoclonal antibody</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Proteasome Inhibitors - pharmacology</topic><topic>Protein localization</topic><topic>Protein Methyltransferases - genetics</topic><topic>Protein Methyltransferases - metabolism</topic><topic>Receptors, Cytoplasmic and Nuclear - antagonists & inhibitors</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Deletion</topic><topic>SETDB1</topic><topic>Subcellular Fractions - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tachibana, Keisuke</creatorcontrib><creatorcontrib>Gotoh, Eiko</creatorcontrib><creatorcontrib>Kawamata, Natsuko</creatorcontrib><creatorcontrib>Ishimoto, Kenji</creatorcontrib><creatorcontrib>Uchihara, Yoshie</creatorcontrib><creatorcontrib>Iwanari, Hiroko</creatorcontrib><creatorcontrib>Sugiyama, Akira</creatorcontrib><creatorcontrib>Kawamura, Takeshi</creatorcontrib><creatorcontrib>Mochizuki, Yasuhiro</creatorcontrib><creatorcontrib>Tanaka, Toshiya</creatorcontrib><creatorcontrib>Sakai, Juro</creatorcontrib><creatorcontrib>Hamakubo, Takao</creatorcontrib><creatorcontrib>Kodama, Tatsuhiko</creatorcontrib><creatorcontrib>Doi, Takefumi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tachibana, Keisuke</au><au>Gotoh, Eiko</au><au>Kawamata, Natsuko</au><au>Ishimoto, Kenji</au><au>Uchihara, Yoshie</au><au>Iwanari, Hiroko</au><au>Sugiyama, Akira</au><au>Kawamura, Takeshi</au><au>Mochizuki, Yasuhiro</au><au>Tanaka, Toshiya</au><au>Sakai, Juro</au><au>Hamakubo, Takao</au><au>Kodama, Tatsuhiko</au><au>Doi, Takefumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the subcellular localization of the human histone methyltransferase SETDB1</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2015-10-02</date><risdate>2015</risdate><volume>465</volume><issue>4</issue><spage>725</spage><epage>731</epage><pages>725-731</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>SET domain, bifurcated 1 (SETDB1) is a histone methyltransferase that methylates lysine 9 on histone H3. Although it is important to know the localization of proteins to elucidate their physiological function, little is known of the subcellular localization of human SETDB1. In the present study, to investigate the subcellular localization of hSETDB1, we established a human cell line constitutively expressing enhanced green fluorescent protein fused to hSETDB1. We then generated a monoclonal antibody against the hSETDB1 protein. Expression of both exogenous and endogenous hSETDB1 was observed mainly in the cytoplasm of various human cell lines. Combined treatment with the nuclear export inhibitor leptomycin B and the proteasome inhibitor MG132 led to the accumulation of hSETDB1 in the nucleus. These findings suggest that hSETDB1, localized in the nucleus, might undergo degradation by the proteasome and be exported to the cytosol, resulting in its detection mainly in the cytosol.
•Endogenous human SETDB1 was localized mainly in the cytoplasm.•Combined treatment with LMB and MG132 led to accumulation of human SETDB1 in the nucleus.•HeLa cells expressing EFGP-hSETDB1 are useful for subcellular localization analyses.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>26296461</pmid><doi>10.1016/j.bbrc.2015.08.065</doi><tpages>7</tpages></addata></record> |
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| subjects | 60 APPLIED LIFE SCIENCES Active Transport, Cell Nucleus - drug effects Amino Acid Sequence BUILDUP Cell Line CELL NUCLEI Cell Nucleus - metabolism CHROMOSOMES CYTOPLASM Cytoplasm - metabolism Exportin 1 Protein Fatty Acids, Unsaturated - pharmacology FLUORESCENCE Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism HEK293 Cells HELA CELLS Hep G2 Cells Histone methyltransferase Histone-Lysine N-Methyltransferase HISTONES HUMAN POPULATIONS Humans Karyopherins - antagonists & inhibitors Leupeptins - pharmacology LYSINE METHYL TRANSFERASES Molecular Sequence Data MONOCLONAL ANTIBODIES Monoclonal antibody Proteasome Endopeptidase Complex - metabolism Proteasome Inhibitors - pharmacology Protein localization Protein Methyltransferases - genetics Protein Methyltransferases - metabolism Receptors, Cytoplasmic and Nuclear - antagonists & inhibitors Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Sequence Deletion SETDB1 Subcellular Fractions - metabolism |
| title | Analysis of the subcellular localization of the human histone methyltransferase SETDB1 |
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