Identification and characterization of FHL3 as a novel angiogenin-binding partner
Angiogenin (Ang) is known to induce cell proliferation and inhibit apoptosis by cellular signaling pathways and by direct nuclear functions of Ang, but the mechanism of action for Ang is not yet clear. The aim of present study was to identify novel binding partner of Ang and to explore the underlyin...
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| Veröffentlicht in: | Gene 2012-08, Vol.504 (2), p.233-237 |
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| creator | Xia, Wenrong Fu, Wenliang Cai, Ling Kong, Haibo Cai, Xin Liu, Jing Wang, Yuanyuan Zou, Minji Xu, Donggang |
| description | Angiogenin (Ang) is known to induce cell proliferation and inhibit apoptosis by cellular signaling pathways and by direct nuclear functions of Ang, but the mechanism of action for Ang is not yet clear. The aim of present study was to identify novel binding partner of Ang and to explore the underlying mechanism. With the use of yeast two-hybrid screening system, Ang was used as the bait to screen human fetal hepatic cDNA library for interacting proteins. Four and a half LIM domains 3 (FHL3) was identified as a novel Ang binding partner. The interaction between Ang and the full length FHL3 was further confirmed by yeast two-hybrid assay, co-immunoprecipitation and GST pull-down assays. Furthermore, FHL3 was required for Ang-mediated HeLa cell proliferation and nuclear translocation of Ang. These findings suggest that the interaction between Ang and FHL3 may provide some clues to the mechanisms of Ang-regulated cell growth and apoptosis.
► A novel binding partner of Ang is discovered by yeast two-hybrid screening assay. ► The interaction between FHL3 and Ang was confirmed by yeast two-hybird assay. ► Ang interacts with FHL3 in vivo. ► Ang interacts with FHL3 directly in vitro. ► FHL3 is required for Ang-stimulated cell proliferation. |
| doi_str_mv | 10.1016/j.gene.2012.05.019 |
| format | Article |
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► A novel binding partner of Ang is discovered by yeast two-hybrid screening assay. ► The interaction between FHL3 and Ang was confirmed by yeast two-hybird assay. ► Ang interacts with FHL3 in vivo. ► Ang interacts with FHL3 directly in vitro. ► FHL3 is required for Ang-stimulated cell proliferation.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/j.gene.2012.05.019</identifier><identifier>PMID: 22633874</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Angiogenin ; Apoptosis ; Base Sequence ; cDNA libraries ; cell growth ; Cell proliferation ; complementary DNA ; DNA Primers ; Fetuses ; FHL3 ; HeLa Cells ; Humans ; Immunoprecipitation ; Interaction ; Intracellular Signaling Peptides and Proteins - genetics ; Intracellular Signaling Peptides and Proteins - metabolism ; LIM Domain Proteins - genetics ; LIM Domain Proteins - metabolism ; Liver ; mechanism of action ; Nuclear transport ; Protein Binding ; proteins ; Ribonuclease, Pancreatic - metabolism ; screening ; Signal transduction ; Two-Hybrid System Techniques ; Yeast two-hybrid</subject><ispartof>Gene, 2012-08, Vol.504 (2), p.233-237</ispartof><rights>2012 Elsevier B.V.</rights><rights>Copyright © 2012 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-c25e5667e1fc56f60fe1a96bc55c79bb07c5c8c44296aacef9078e1c205514603</citedby><cites>FETCH-LOGICAL-c413t-c25e5667e1fc56f60fe1a96bc55c79bb07c5c8c44296aacef9078e1c205514603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S037811191200594X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22633874$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xia, Wenrong</creatorcontrib><creatorcontrib>Fu, Wenliang</creatorcontrib><creatorcontrib>Cai, Ling</creatorcontrib><creatorcontrib>Kong, Haibo</creatorcontrib><creatorcontrib>Cai, Xin</creatorcontrib><creatorcontrib>Liu, Jing</creatorcontrib><creatorcontrib>Wang, Yuanyuan</creatorcontrib><creatorcontrib>Zou, Minji</creatorcontrib><creatorcontrib>Xu, Donggang</creatorcontrib><title>Identification and characterization of FHL3 as a novel angiogenin-binding partner</title><title>Gene</title><addtitle>Gene</addtitle><description>Angiogenin (Ang) is known to induce cell proliferation and inhibit apoptosis by cellular signaling pathways and by direct nuclear functions of Ang, but the mechanism of action for Ang is not yet clear. The aim of present study was to identify novel binding partner of Ang and to explore the underlying mechanism. With the use of yeast two-hybrid screening system, Ang was used as the bait to screen human fetal hepatic cDNA library for interacting proteins. Four and a half LIM domains 3 (FHL3) was identified as a novel Ang binding partner. The interaction between Ang and the full length FHL3 was further confirmed by yeast two-hybrid assay, co-immunoprecipitation and GST pull-down assays. Furthermore, FHL3 was required for Ang-mediated HeLa cell proliferation and nuclear translocation of Ang. These findings suggest that the interaction between Ang and FHL3 may provide some clues to the mechanisms of Ang-regulated cell growth and apoptosis.
► A novel binding partner of Ang is discovered by yeast two-hybrid screening assay. ► The interaction between FHL3 and Ang was confirmed by yeast two-hybird assay. ► Ang interacts with FHL3 in vivo. ► Ang interacts with FHL3 directly in vitro. ► FHL3 is required for Ang-stimulated cell proliferation.</description><subject>Angiogenin</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>cDNA libraries</subject><subject>cell growth</subject><subject>Cell proliferation</subject><subject>complementary DNA</subject><subject>DNA Primers</subject><subject>Fetuses</subject><subject>FHL3</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Interaction</subject><subject>Intracellular Signaling Peptides and Proteins - genetics</subject><subject>Intracellular Signaling Peptides and Proteins - metabolism</subject><subject>LIM Domain Proteins - genetics</subject><subject>LIM Domain Proteins - metabolism</subject><subject>Liver</subject><subject>mechanism of action</subject><subject>Nuclear transport</subject><subject>Protein Binding</subject><subject>proteins</subject><subject>Ribonuclease, Pancreatic - metabolism</subject><subject>screening</subject><subject>Signal transduction</subject><subject>Two-Hybrid System Techniques</subject><subject>Yeast two-hybrid</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi1ERZfCH-AAOXJJ8Ef8EYkLqlpaaSVUtT1bzmS8eLVrL3a2Evx6vErhiPBlJOuZdzyPCXnHaMcoU5-23QYjdpwy3lHZUTa8ICtm9NBSKsxLsqJCm5YxNpyT16VsaT1S8lfknHMlhNH9itzdThjn4AO4OaTYuDg18N1lBzPm8Gu5TL65vlmLxpXGNTE94a5ym5Dq-BDbMcQpxE1zcHmOmN-QM-92Bd8-1wvyeH31cHnTrr99vb38sm6hZ2JugUuUSmlkHqTyinpkblAjSAl6GEeqQYKBvueDcg7QD1QbZMDrCqxXVFyQj0vuIacfRyyz3YcCuNu5iOlYLKO8V0r1Rv8PyoUelDQV5QsKOZWS0dtDDnuXf1bInqzbrT1Ztyfrlkpbrdem98_5x3GP09-WP5or8GEBvEvWbXIo9vG-Jsj6I72Q5rTN54XAquwpYLYFAkbAKWSE2U4p_OsFvwHut5te</recordid><startdate>20120810</startdate><enddate>20120810</enddate><creator>Xia, Wenrong</creator><creator>Fu, Wenliang</creator><creator>Cai, Ling</creator><creator>Kong, Haibo</creator><creator>Cai, Xin</creator><creator>Liu, Jing</creator><creator>Wang, Yuanyuan</creator><creator>Zou, Minji</creator><creator>Xu, Donggang</creator><general>Elsevier B.V</general><scope>FBQ</scope><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><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20120810</creationdate><title>Identification and characterization of FHL3 as a novel angiogenin-binding partner</title><author>Xia, Wenrong ; Fu, Wenliang ; Cai, Ling ; Kong, Haibo ; Cai, Xin ; Liu, Jing ; Wang, Yuanyuan ; Zou, Minji ; Xu, Donggang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-c25e5667e1fc56f60fe1a96bc55c79bb07c5c8c44296aacef9078e1c205514603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Angiogenin</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>cDNA libraries</topic><topic>cell growth</topic><topic>Cell proliferation</topic><topic>complementary DNA</topic><topic>DNA Primers</topic><topic>Fetuses</topic><topic>FHL3</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Interaction</topic><topic>Intracellular Signaling Peptides and Proteins - genetics</topic><topic>Intracellular Signaling Peptides and Proteins - metabolism</topic><topic>LIM Domain Proteins - genetics</topic><topic>LIM Domain Proteins - metabolism</topic><topic>Liver</topic><topic>mechanism of action</topic><topic>Nuclear transport</topic><topic>Protein Binding</topic><topic>proteins</topic><topic>Ribonuclease, Pancreatic - metabolism</topic><topic>screening</topic><topic>Signal transduction</topic><topic>Two-Hybrid System Techniques</topic><topic>Yeast two-hybrid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xia, Wenrong</creatorcontrib><creatorcontrib>Fu, Wenliang</creatorcontrib><creatorcontrib>Cai, Ling</creatorcontrib><creatorcontrib>Kong, Haibo</creatorcontrib><creatorcontrib>Cai, Xin</creatorcontrib><creatorcontrib>Liu, Jing</creatorcontrib><creatorcontrib>Wang, Yuanyuan</creatorcontrib><creatorcontrib>Zou, Minji</creatorcontrib><creatorcontrib>Xu, Donggang</creatorcontrib><collection>AGRIS</collection><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><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xia, Wenrong</au><au>Fu, Wenliang</au><au>Cai, Ling</au><au>Kong, Haibo</au><au>Cai, Xin</au><au>Liu, Jing</au><au>Wang, Yuanyuan</au><au>Zou, Minji</au><au>Xu, Donggang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of FHL3 as a novel angiogenin-binding partner</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>2012-08-10</date><risdate>2012</risdate><volume>504</volume><issue>2</issue><spage>233</spage><epage>237</epage><pages>233-237</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><abstract>Angiogenin (Ang) is known to induce cell proliferation and inhibit apoptosis by cellular signaling pathways and by direct nuclear functions of Ang, but the mechanism of action for Ang is not yet clear. The aim of present study was to identify novel binding partner of Ang and to explore the underlying mechanism. With the use of yeast two-hybrid screening system, Ang was used as the bait to screen human fetal hepatic cDNA library for interacting proteins. Four and a half LIM domains 3 (FHL3) was identified as a novel Ang binding partner. The interaction between Ang and the full length FHL3 was further confirmed by yeast two-hybrid assay, co-immunoprecipitation and GST pull-down assays. Furthermore, FHL3 was required for Ang-mediated HeLa cell proliferation and nuclear translocation of Ang. These findings suggest that the interaction between Ang and FHL3 may provide some clues to the mechanisms of Ang-regulated cell growth and apoptosis.
► A novel binding partner of Ang is discovered by yeast two-hybrid screening assay. ► The interaction between FHL3 and Ang was confirmed by yeast two-hybird assay. ► Ang interacts with FHL3 in vivo. ► Ang interacts with FHL3 directly in vitro. ► FHL3 is required for Ang-stimulated cell proliferation.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>22633874</pmid><doi>10.1016/j.gene.2012.05.019</doi><tpages>5</tpages></addata></record> |
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| subjects | Angiogenin Apoptosis Base Sequence cDNA libraries cell growth Cell proliferation complementary DNA DNA Primers Fetuses FHL3 HeLa Cells Humans Immunoprecipitation Interaction Intracellular Signaling Peptides and Proteins - genetics Intracellular Signaling Peptides and Proteins - metabolism LIM Domain Proteins - genetics LIM Domain Proteins - metabolism Liver mechanism of action Nuclear transport Protein Binding proteins Ribonuclease, Pancreatic - metabolism screening Signal transduction Two-Hybrid System Techniques Yeast two-hybrid |
| title | Identification and characterization of FHL3 as a novel angiogenin-binding partner |
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