TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of ElK-1 and AP-1
The tripartite motif (TRIM) proteins play important roles in a variety of cellular functions including cell proliferation, differentiation, development, oncogenesis, and apoptosis. In this study, we report the identification and characterization of the human tripartite motif-containing protein 45 (...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2004-10, Vol.323 (1), p.9-16 |
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| creator | Wang, Yuequn Li, Yongqing Qi, Xinzhu Yuan, Wuzhou Ai, Jianping Zhu, Chuanbing Cao, Lei Yang, Hong Liu, Fang Wu, Xiushan Liu, Mingyao |
| description | The tripartite motif (TRIM) proteins play important roles in a variety of cellular functions including cell proliferation, differentiation, development, oncogenesis, and apoptosis. In this study, we report the identification and characterization of the human tripartite motif-containing protein 45 (
TRIM45), a novel member of the TRIM family, from a human embryonic heart cDNA library. TRIM45 has a predicted 580 amino acid open reading frame, encoding a putative 64-kDa protein. The N-terminal region harbors a RING finger, two B-boxes, and a predicted α-helical coiled-coil domain, which together form the RBCC/TRIM motif found in a large family of proteins, whereas the C-terminal region contains a filamin-type immunoglobulin (IG-FLMN) domain. Northern blot analysis indicates that
TRIM45 is expressed in a variety of human adult and embryonic tissues. In the cell, TRIM45 protein is expressed both in cytoplasm and in cell nucleus. Overexpression of TRIM45 in COS-7 cells inhibits the transcriptional activities of ElK-1 and AP-1. These results suggest that TRIM45 may act as a new transcriptional repressor in mitogen-activated protein kinase signaling pathway. |
| doi_str_mv | 10.1016/j.bbrc.2004.08.048 |
| format | Article |
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TRIM45), a novel member of the TRIM family, from a human embryonic heart cDNA library. TRIM45 has a predicted 580 amino acid open reading frame, encoding a putative 64-kDa protein. The N-terminal region harbors a RING finger, two B-boxes, and a predicted α-helical coiled-coil domain, which together form the RBCC/TRIM motif found in a large family of proteins, whereas the C-terminal region contains a filamin-type immunoglobulin (IG-FLMN) domain. Northern blot analysis indicates that
TRIM45 is expressed in a variety of human adult and embryonic tissues. In the cell, TRIM45 protein is expressed both in cytoplasm and in cell nucleus. Overexpression of TRIM45 in COS-7 cells inhibits the transcriptional activities of ElK-1 and AP-1. These results suggest that TRIM45 may act as a new transcriptional repressor in mitogen-activated protein kinase signaling pathway.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2004.08.048</identifier><identifier>PMID: 15351693</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Apoptosis ; Base Sequence ; Blotting, Northern ; Cell Differentiation ; Cell Division ; Cell Nucleus - metabolism ; Cloning, Molecular ; Computational Biology ; COS Cells ; Cytoplasm - metabolism ; DNA, Complementary - metabolism ; DNA-Binding Proteins - metabolism ; Elk-1 ; ets-Domain Protein Elk-1 ; Exons ; Gene Library ; Genes, Reporter ; Humans ; MAP Kinase Signaling System ; MAPK signaling pathway ; Molecular Sequence Data ; Myocardium - metabolism ; Open Reading Frames ; Phylogeny ; Protein Structure, Tertiary ; Proto-Oncogene Proteins - metabolism ; RBCC/TRIM proteins ; Repressor Proteins - chemistry ; Repressor Proteins - physiology ; RNA - chemistry ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; Signal Transduction ; Tissue Distribution ; Transcription Factor AP-1 - metabolism ; Transcription factor repressor ; Transcription Factors - metabolism ; Transcription, Genetic ; Transcriptional Activation ; Transfection ; TRIM45</subject><ispartof>Biochemical and biophysical research communications, 2004-10, Vol.323 (1), p.9-16</ispartof><rights>2004 Elsevier Inc.</rights><rights>Copyright 2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c383t-bcbcec451ddb1843640e87812b37bc562a9287371afe205e5e512085f17daba23</citedby><cites>FETCH-LOGICAL-c383t-bcbcec451ddb1843640e87812b37bc562a9287371afe205e5e512085f17daba23</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.2004.08.048$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15351693$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Yuequn</creatorcontrib><creatorcontrib>Li, Yongqing</creatorcontrib><creatorcontrib>Qi, Xinzhu</creatorcontrib><creatorcontrib>Yuan, Wuzhou</creatorcontrib><creatorcontrib>Ai, Jianping</creatorcontrib><creatorcontrib>Zhu, Chuanbing</creatorcontrib><creatorcontrib>Cao, Lei</creatorcontrib><creatorcontrib>Yang, Hong</creatorcontrib><creatorcontrib>Liu, Fang</creatorcontrib><creatorcontrib>Wu, Xiushan</creatorcontrib><creatorcontrib>Liu, Mingyao</creatorcontrib><title>TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of ElK-1 and AP-1</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The tripartite motif (TRIM) proteins play important roles in a variety of cellular functions including cell proliferation, differentiation, development, oncogenesis, and apoptosis. In this study, we report the identification and characterization of the human tripartite motif-containing protein 45 (
TRIM45), a novel member of the TRIM family, from a human embryonic heart cDNA library. TRIM45 has a predicted 580 amino acid open reading frame, encoding a putative 64-kDa protein. The N-terminal region harbors a RING finger, two B-boxes, and a predicted α-helical coiled-coil domain, which together form the RBCC/TRIM motif found in a large family of proteins, whereas the C-terminal region contains a filamin-type immunoglobulin (IG-FLMN) domain. Northern blot analysis indicates that
TRIM45 is expressed in a variety of human adult and embryonic tissues. In the cell, TRIM45 protein is expressed both in cytoplasm and in cell nucleus. Overexpression of TRIM45 in COS-7 cells inhibits the transcriptional activities of ElK-1 and AP-1. These results suggest that TRIM45 may act as a new transcriptional repressor in mitogen-activated protein kinase signaling pathway.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Cell Differentiation</subject><subject>Cell Division</subject><subject>Cell Nucleus - metabolism</subject><subject>Cloning, Molecular</subject><subject>Computational Biology</subject><subject>COS Cells</subject><subject>Cytoplasm - metabolism</subject><subject>DNA, Complementary - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Elk-1</subject><subject>ets-Domain Protein Elk-1</subject><subject>Exons</subject><subject>Gene Library</subject><subject>Genes, Reporter</subject><subject>Humans</subject><subject>MAP Kinase Signaling System</subject><subject>MAPK signaling pathway</subject><subject>Molecular Sequence Data</subject><subject>Myocardium - metabolism</subject><subject>Open Reading Frames</subject><subject>Phylogeny</subject><subject>Protein Structure, Tertiary</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>RBCC/TRIM proteins</subject><subject>Repressor Proteins - chemistry</subject><subject>Repressor Proteins - physiology</subject><subject>RNA - chemistry</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction</subject><subject>Tissue Distribution</subject><subject>Transcription Factor AP-1 - metabolism</subject><subject>Transcription factor repressor</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic</subject><subject>Transcriptional Activation</subject><subject>Transfection</subject><subject>TRIM45</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFu1DAQhi0EotvCC3BAPnFq0hnbcRyJS1mVUlEEqorECct2HNWrrLPY3pV4exLtStxAc5jDfPPP6CPkDUKNgPJqU1ubXM0ARA2qBqGekRVCBxVDEM_JCgBkxTr8cUbOc94AIArZvSRn2PAGZcdX5Ofjw90X0VxSQ-N08CN92m9NpA8f1uurZUR3aSo-xEsa4lOwoWRakonZpbArYYpmpMaVcAgl-Eyngd6MnyukJvb0-luFr8iLwYzZvz71C_L9483j-lN1__X2bn19XzmueKmss8470WDfW1SCSwFetQqZ5a11jWSmY6rlLZrBM2j8XMhANQO2vbGG8Qvy7pg7v_tr73PR25CdH0cT_bTPWkolJOPdf0FsWzXfXUB2BF2ack5-0LsUtib91gh60a83etGvF_0alJ71z0tvT-l7u_X935WT7xl4fwT8LOMQfNLZBR-d70Pyruh-Cv_K_wOxM5N2</recordid><startdate>20041008</startdate><enddate>20041008</enddate><creator>Wang, Yuequn</creator><creator>Li, Yongqing</creator><creator>Qi, Xinzhu</creator><creator>Yuan, Wuzhou</creator><creator>Ai, Jianping</creator><creator>Zhu, Chuanbing</creator><creator>Cao, Lei</creator><creator>Yang, Hong</creator><creator>Liu, Fang</creator><creator>Wu, Xiushan</creator><creator>Liu, Mingyao</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20041008</creationdate><title>TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of ElK-1 and AP-1</title><author>Wang, Yuequn ; Li, Yongqing ; Qi, Xinzhu ; Yuan, Wuzhou ; Ai, Jianping ; Zhu, Chuanbing ; Cao, Lei ; Yang, Hong ; Liu, Fang ; Wu, Xiushan ; Liu, Mingyao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c383t-bcbcec451ddb1843640e87812b37bc562a9287371afe205e5e512085f17daba23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Cell Differentiation</topic><topic>Cell Division</topic><topic>Cell Nucleus - metabolism</topic><topic>Cloning, Molecular</topic><topic>Computational Biology</topic><topic>COS Cells</topic><topic>Cytoplasm - metabolism</topic><topic>DNA, Complementary - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Elk-1</topic><topic>ets-Domain Protein Elk-1</topic><topic>Exons</topic><topic>Gene Library</topic><topic>Genes, Reporter</topic><topic>Humans</topic><topic>MAP Kinase Signaling System</topic><topic>MAPK signaling pathway</topic><topic>Molecular Sequence Data</topic><topic>Myocardium - metabolism</topic><topic>Open Reading Frames</topic><topic>Phylogeny</topic><topic>Protein Structure, Tertiary</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>RBCC/TRIM proteins</topic><topic>Repressor Proteins - chemistry</topic><topic>Repressor Proteins - physiology</topic><topic>RNA - chemistry</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction</topic><topic>Tissue Distribution</topic><topic>Transcription Factor AP-1 - metabolism</topic><topic>Transcription factor repressor</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><topic>Transcriptional Activation</topic><topic>Transfection</topic><topic>TRIM45</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Yuequn</creatorcontrib><creatorcontrib>Li, Yongqing</creatorcontrib><creatorcontrib>Qi, Xinzhu</creatorcontrib><creatorcontrib>Yuan, Wuzhou</creatorcontrib><creatorcontrib>Ai, Jianping</creatorcontrib><creatorcontrib>Zhu, Chuanbing</creatorcontrib><creatorcontrib>Cao, Lei</creatorcontrib><creatorcontrib>Yang, Hong</creatorcontrib><creatorcontrib>Liu, Fang</creatorcontrib><creatorcontrib>Wu, Xiushan</creatorcontrib><creatorcontrib>Liu, Mingyao</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Yuequn</au><au>Li, Yongqing</au><au>Qi, Xinzhu</au><au>Yuan, Wuzhou</au><au>Ai, Jianping</au><au>Zhu, Chuanbing</au><au>Cao, Lei</au><au>Yang, Hong</au><au>Liu, Fang</au><au>Wu, Xiushan</au><au>Liu, Mingyao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of ElK-1 and AP-1</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2004-10-08</date><risdate>2004</risdate><volume>323</volume><issue>1</issue><spage>9</spage><epage>16</epage><pages>9-16</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The tripartite motif (TRIM) proteins play important roles in a variety of cellular functions including cell proliferation, differentiation, development, oncogenesis, and apoptosis. In this study, we report the identification and characterization of the human tripartite motif-containing protein 45 (
TRIM45), a novel member of the TRIM family, from a human embryonic heart cDNA library. TRIM45 has a predicted 580 amino acid open reading frame, encoding a putative 64-kDa protein. The N-terminal region harbors a RING finger, two B-boxes, and a predicted α-helical coiled-coil domain, which together form the RBCC/TRIM motif found in a large family of proteins, whereas the C-terminal region contains a filamin-type immunoglobulin (IG-FLMN) domain. Northern blot analysis indicates that
TRIM45 is expressed in a variety of human adult and embryonic tissues. In the cell, TRIM45 protein is expressed both in cytoplasm and in cell nucleus. Overexpression of TRIM45 in COS-7 cells inhibits the transcriptional activities of ElK-1 and AP-1. These results suggest that TRIM45 may act as a new transcriptional repressor in mitogen-activated protein kinase signaling pathway.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15351693</pmid><doi>10.1016/j.bbrc.2004.08.048</doi><tpages>8</tpages></addata></record> |
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| subjects | Amino Acid Motifs Amino Acid Sequence Animals Apoptosis Base Sequence Blotting, Northern Cell Differentiation Cell Division Cell Nucleus - metabolism Cloning, Molecular Computational Biology COS Cells Cytoplasm - metabolism DNA, Complementary - metabolism DNA-Binding Proteins - metabolism Elk-1 ets-Domain Protein Elk-1 Exons Gene Library Genes, Reporter Humans MAP Kinase Signaling System MAPK signaling pathway Molecular Sequence Data Myocardium - metabolism Open Reading Frames Phylogeny Protein Structure, Tertiary Proto-Oncogene Proteins - metabolism RBCC/TRIM proteins Repressor Proteins - chemistry Repressor Proteins - physiology RNA - chemistry RNA, Messenger - metabolism Sequence Homology, Amino Acid Signal Transduction Tissue Distribution Transcription Factor AP-1 - metabolism Transcription factor repressor Transcription Factors - metabolism Transcription, Genetic Transcriptional Activation Transfection TRIM45 |
| title | TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of ElK-1 and AP-1 |
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