Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation
Humoral autoimmunity paralleled by the accumulation of follicular helper T cells (T(FH) cells) is linked to mutation of the gene encoding the RNA-binding protein roquin-1. Here we found that T cells lacking roquin caused pathology in the lung and accumulated as cells of the T(H)17 subset of helper T...
Gespeichert in:
| Veröffentlicht in: | Nature immunology 2014-11, Vol.15 (11), p.1079 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 11 |
| container_start_page | 1079 |
| container_title | Nature immunology |
| container_volume | 15 |
| creator | Jeltsch, Katharina M Hu, Desheng Brenner, Sven Zöller, Jessica Heinz, Gitta A Nagel, Daniel Vogel, Katharina U Rehage, Nina Warth, Sebastian C Edelmann, Stephanie L Gloury, Renee Martin, Nina Lohs, Claudia Lech, Maciej Stehklein, Jenny E Geerlof, Arie Kremmer, Elisabeth Weber, Achim Anders, Hans-Joachim Schmitz, Ingo Schmidt-Supprian, Marc Fu, Mingui Holtmann, Helmut Krappmann, Daniel Ruland, Jürgen Kallies, Axel Heikenwalder, Mathias Heissmeyer, Vigo |
| description | Humoral autoimmunity paralleled by the accumulation of follicular helper T cells (T(FH) cells) is linked to mutation of the gene encoding the RNA-binding protein roquin-1. Here we found that T cells lacking roquin caused pathology in the lung and accumulated as cells of the T(H)17 subset of helper T cells in the lungs. Roquin inhibited T(H)17 cell differentiation and acted together with the endoribonuclease regnase-1 to repress target mRNA encoding the T(H)17 cell-promoting factors IL-6, ICOS, c-Rel, IRF4, IκBNS and IκBζ. This cooperation required binding of RNA by roquin and the nuclease activity of regnase-1. Upon recognition of antigen by the T cell antigen receptor (TCR), roquin and regnase-1 proteins were cleaved by the paracaspase MALT1. Thus, this pathway acts as a 'rheostat' by translating TCR signal strength via graded inactivation of post-transcriptional repressors and differential derepression of targets to enhance T(H)17 differentiation. |
| doi_str_mv | 10.1038/ni.3008 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed</sourceid><recordid>TN_cdi_pubmed_primary_25282160</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>25282160</sourcerecordid><originalsourceid>FETCH-LOGICAL-p141t-3b36c667946971854530032435f919a40db6d8295414f22a102edd1ab785896a3</originalsourceid><addsrcrecordid>eNo1UMtKAzEUDYLYWsU_kCx1MZqbZDKTZSlqhYqbui53mjt1pJ3EJC30F_xqR9TVgfOCcxi7AnEHQtX3fXenhKhP2BhKaQtpwYzYeUofQoCujD5jI1nKWoIRY_Y12xIecEPctzz6z33Xc-wdj7TpMVEBvDny_E48YMQ1pjCQ_GW6WMJgGaKJ0o_cRb72PlDE3B1oexzEECklcjxj3FAeXJ6H6Hc-E1_ezG-h4q5rW4rU525I-f6Cnba4TXT5hxP29viwnM2LxevT82y6KAJoyIVqlFkbU1ltbAV1qcthrZJala0Fi1q4xrha2lKDbqVEEJKcA2yquqytQTVh17-9Yd_syK1C7HYYj6v_U9Q3-PBgeQ</addsrcrecordid><sourcetype>Index Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><source>Nature</source><creator>Jeltsch, Katharina M ; Hu, Desheng ; Brenner, Sven ; Zöller, Jessica ; Heinz, Gitta A ; Nagel, Daniel ; Vogel, Katharina U ; Rehage, Nina ; Warth, Sebastian C ; Edelmann, Stephanie L ; Gloury, Renee ; Martin, Nina ; Lohs, Claudia ; Lech, Maciej ; Stehklein, Jenny E ; Geerlof, Arie ; Kremmer, Elisabeth ; Weber, Achim ; Anders, Hans-Joachim ; Schmitz, Ingo ; Schmidt-Supprian, Marc ; Fu, Mingui ; Holtmann, Helmut ; Krappmann, Daniel ; Ruland, Jürgen ; Kallies, Axel ; Heikenwalder, Mathias ; Heissmeyer, Vigo</creator><creatorcontrib>Jeltsch, Katharina M ; Hu, Desheng ; Brenner, Sven ; Zöller, Jessica ; Heinz, Gitta A ; Nagel, Daniel ; Vogel, Katharina U ; Rehage, Nina ; Warth, Sebastian C ; Edelmann, Stephanie L ; Gloury, Renee ; Martin, Nina ; Lohs, Claudia ; Lech, Maciej ; Stehklein, Jenny E ; Geerlof, Arie ; Kremmer, Elisabeth ; Weber, Achim ; Anders, Hans-Joachim ; Schmitz, Ingo ; Schmidt-Supprian, Marc ; Fu, Mingui ; Holtmann, Helmut ; Krappmann, Daniel ; Ruland, Jürgen ; Kallies, Axel ; Heikenwalder, Mathias ; Heissmeyer, Vigo</creatorcontrib><description>Humoral autoimmunity paralleled by the accumulation of follicular helper T cells (T(FH) cells) is linked to mutation of the gene encoding the RNA-binding protein roquin-1. Here we found that T cells lacking roquin caused pathology in the lung and accumulated as cells of the T(H)17 subset of helper T cells in the lungs. Roquin inhibited T(H)17 cell differentiation and acted together with the endoribonuclease regnase-1 to repress target mRNA encoding the T(H)17 cell-promoting factors IL-6, ICOS, c-Rel, IRF4, IκBNS and IκBζ. This cooperation required binding of RNA by roquin and the nuclease activity of regnase-1. Upon recognition of antigen by the T cell antigen receptor (TCR), roquin and regnase-1 proteins were cleaved by the paracaspase MALT1. Thus, this pathway acts as a 'rheostat' by translating TCR signal strength via graded inactivation of post-transcriptional repressors and differential derepression of targets to enhance T(H)17 differentiation.</description><identifier>EISSN: 1529-2916</identifier><identifier>DOI: 10.1038/ni.3008</identifier><identifier>PMID: 25282160</identifier><language>eng</language><publisher>United States</publisher><subject>Adaptor Proteins, Signal Transducing - genetics ; Amino Acid Sequence ; Animals ; Binding Sites - immunology ; Caspases - metabolism ; Cell Differentiation - immunology ; Cell Line ; Genes, rel - genetics ; HEK293 Cells ; Humans ; Inducible T-Cell Co-Stimulator Protein - genetics ; Interferon Regulatory Factors - genetics ; Interleukin-6 - genetics ; Intracellular Signaling Peptides and Proteins ; Lung - immunology ; Lung - pathology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Inbred NOD ; Mice, Knockout ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein ; Neoplasm Proteins - metabolism ; Nuclear Proteins - genetics ; Proteins - genetics ; Receptors, Antigen, T-Cell - immunology ; Ribonucleases - metabolism ; RNA, Messenger - genetics ; RNA-Binding Proteins - metabolism ; Sequence Alignment ; Th17 Cells - cytology ; Th17 Cells - immunology ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism</subject><ispartof>Nature immunology, 2014-11, Vol.15 (11), p.1079</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000000157713907 ; 0000000253600419</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25282160$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jeltsch, Katharina M</creatorcontrib><creatorcontrib>Hu, Desheng</creatorcontrib><creatorcontrib>Brenner, Sven</creatorcontrib><creatorcontrib>Zöller, Jessica</creatorcontrib><creatorcontrib>Heinz, Gitta A</creatorcontrib><creatorcontrib>Nagel, Daniel</creatorcontrib><creatorcontrib>Vogel, Katharina U</creatorcontrib><creatorcontrib>Rehage, Nina</creatorcontrib><creatorcontrib>Warth, Sebastian C</creatorcontrib><creatorcontrib>Edelmann, Stephanie L</creatorcontrib><creatorcontrib>Gloury, Renee</creatorcontrib><creatorcontrib>Martin, Nina</creatorcontrib><creatorcontrib>Lohs, Claudia</creatorcontrib><creatorcontrib>Lech, Maciej</creatorcontrib><creatorcontrib>Stehklein, Jenny E</creatorcontrib><creatorcontrib>Geerlof, Arie</creatorcontrib><creatorcontrib>Kremmer, Elisabeth</creatorcontrib><creatorcontrib>Weber, Achim</creatorcontrib><creatorcontrib>Anders, Hans-Joachim</creatorcontrib><creatorcontrib>Schmitz, Ingo</creatorcontrib><creatorcontrib>Schmidt-Supprian, Marc</creatorcontrib><creatorcontrib>Fu, Mingui</creatorcontrib><creatorcontrib>Holtmann, Helmut</creatorcontrib><creatorcontrib>Krappmann, Daniel</creatorcontrib><creatorcontrib>Ruland, Jürgen</creatorcontrib><creatorcontrib>Kallies, Axel</creatorcontrib><creatorcontrib>Heikenwalder, Mathias</creatorcontrib><creatorcontrib>Heissmeyer, Vigo</creatorcontrib><title>Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation</title><title>Nature immunology</title><addtitle>Nat Immunol</addtitle><description>Humoral autoimmunity paralleled by the accumulation of follicular helper T cells (T(FH) cells) is linked to mutation of the gene encoding the RNA-binding protein roquin-1. Here we found that T cells lacking roquin caused pathology in the lung and accumulated as cells of the T(H)17 subset of helper T cells in the lungs. Roquin inhibited T(H)17 cell differentiation and acted together with the endoribonuclease regnase-1 to repress target mRNA encoding the T(H)17 cell-promoting factors IL-6, ICOS, c-Rel, IRF4, IκBNS and IκBζ. This cooperation required binding of RNA by roquin and the nuclease activity of regnase-1. Upon recognition of antigen by the T cell antigen receptor (TCR), roquin and regnase-1 proteins were cleaved by the paracaspase MALT1. Thus, this pathway acts as a 'rheostat' by translating TCR signal strength via graded inactivation of post-transcriptional repressors and differential derepression of targets to enhance T(H)17 differentiation.</description><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites - immunology</subject><subject>Caspases - metabolism</subject><subject>Cell Differentiation - immunology</subject><subject>Cell Line</subject><subject>Genes, rel - genetics</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Inducible T-Cell Co-Stimulator Protein - genetics</subject><subject>Interferon Regulatory Factors - genetics</subject><subject>Interleukin-6 - genetics</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Lung - immunology</subject><subject>Lung - pathology</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Inbred NOD</subject><subject>Mice, Knockout</subject><subject>Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Nuclear Proteins - genetics</subject><subject>Proteins - genetics</subject><subject>Receptors, Antigen, T-Cell - immunology</subject><subject>Ribonucleases - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Th17 Cells - cytology</subject><subject>Th17 Cells - immunology</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><issn>1529-2916</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1UMtKAzEUDYLYWsU_kCx1MZqbZDKTZSlqhYqbui53mjt1pJ3EJC30F_xqR9TVgfOCcxi7AnEHQtX3fXenhKhP2BhKaQtpwYzYeUofQoCujD5jI1nKWoIRY_Y12xIecEPctzz6z33Xc-wdj7TpMVEBvDny_E48YMQ1pjCQ_GW6WMJgGaKJ0o_cRb72PlDE3B1oexzEECklcjxj3FAeXJ6H6Hc-E1_ezG-h4q5rW4rU525I-f6Cnba4TXT5hxP29viwnM2LxevT82y6KAJoyIVqlFkbU1ltbAV1qcthrZJala0Fi1q4xrha2lKDbqVEEJKcA2yquqytQTVh17-9Yd_syK1C7HYYj6v_U9Q3-PBgeQ</recordid><startdate>201411</startdate><enddate>201411</enddate><creator>Jeltsch, Katharina M</creator><creator>Hu, Desheng</creator><creator>Brenner, Sven</creator><creator>Zöller, Jessica</creator><creator>Heinz, Gitta A</creator><creator>Nagel, Daniel</creator><creator>Vogel, Katharina U</creator><creator>Rehage, Nina</creator><creator>Warth, Sebastian C</creator><creator>Edelmann, Stephanie L</creator><creator>Gloury, Renee</creator><creator>Martin, Nina</creator><creator>Lohs, Claudia</creator><creator>Lech, Maciej</creator><creator>Stehklein, Jenny E</creator><creator>Geerlof, Arie</creator><creator>Kremmer, Elisabeth</creator><creator>Weber, Achim</creator><creator>Anders, Hans-Joachim</creator><creator>Schmitz, Ingo</creator><creator>Schmidt-Supprian, Marc</creator><creator>Fu, Mingui</creator><creator>Holtmann, Helmut</creator><creator>Krappmann, Daniel</creator><creator>Ruland, Jürgen</creator><creator>Kallies, Axel</creator><creator>Heikenwalder, Mathias</creator><creator>Heissmeyer, Vigo</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><orcidid>https://orcid.org/0000000157713907</orcidid><orcidid>https://orcid.org/0000000253600419</orcidid></search><sort><creationdate>201411</creationdate><title>Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation</title><author>Jeltsch, Katharina M ; Hu, Desheng ; Brenner, Sven ; Zöller, Jessica ; Heinz, Gitta A ; Nagel, Daniel ; Vogel, Katharina U ; Rehage, Nina ; Warth, Sebastian C ; Edelmann, Stephanie L ; Gloury, Renee ; Martin, Nina ; Lohs, Claudia ; Lech, Maciej ; Stehklein, Jenny E ; Geerlof, Arie ; Kremmer, Elisabeth ; Weber, Achim ; Anders, Hans-Joachim ; Schmitz, Ingo ; Schmidt-Supprian, Marc ; Fu, Mingui ; Holtmann, Helmut ; Krappmann, Daniel ; Ruland, Jürgen ; Kallies, Axel ; Heikenwalder, Mathias ; Heissmeyer, Vigo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p141t-3b36c667946971854530032435f919a40db6d8295414f22a102edd1ab785896a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites - immunology</topic><topic>Caspases - metabolism</topic><topic>Cell Differentiation - immunology</topic><topic>Cell Line</topic><topic>Genes, rel - genetics</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Inducible T-Cell Co-Stimulator Protein - genetics</topic><topic>Interferon Regulatory Factors - genetics</topic><topic>Interleukin-6 - genetics</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Lung - immunology</topic><topic>Lung - pathology</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Inbred NOD</topic><topic>Mice, Knockout</topic><topic>Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Nuclear Proteins - genetics</topic><topic>Proteins - genetics</topic><topic>Receptors, Antigen, T-Cell - immunology</topic><topic>Ribonucleases - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Th17 Cells - cytology</topic><topic>Th17 Cells - immunology</topic><topic>Ubiquitin-Protein Ligases - genetics</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jeltsch, Katharina M</creatorcontrib><creatorcontrib>Hu, Desheng</creatorcontrib><creatorcontrib>Brenner, Sven</creatorcontrib><creatorcontrib>Zöller, Jessica</creatorcontrib><creatorcontrib>Heinz, Gitta A</creatorcontrib><creatorcontrib>Nagel, Daniel</creatorcontrib><creatorcontrib>Vogel, Katharina U</creatorcontrib><creatorcontrib>Rehage, Nina</creatorcontrib><creatorcontrib>Warth, Sebastian C</creatorcontrib><creatorcontrib>Edelmann, Stephanie L</creatorcontrib><creatorcontrib>Gloury, Renee</creatorcontrib><creatorcontrib>Martin, Nina</creatorcontrib><creatorcontrib>Lohs, Claudia</creatorcontrib><creatorcontrib>Lech, Maciej</creatorcontrib><creatorcontrib>Stehklein, Jenny E</creatorcontrib><creatorcontrib>Geerlof, Arie</creatorcontrib><creatorcontrib>Kremmer, Elisabeth</creatorcontrib><creatorcontrib>Weber, Achim</creatorcontrib><creatorcontrib>Anders, Hans-Joachim</creatorcontrib><creatorcontrib>Schmitz, Ingo</creatorcontrib><creatorcontrib>Schmidt-Supprian, Marc</creatorcontrib><creatorcontrib>Fu, Mingui</creatorcontrib><creatorcontrib>Holtmann, Helmut</creatorcontrib><creatorcontrib>Krappmann, Daniel</creatorcontrib><creatorcontrib>Ruland, Jürgen</creatorcontrib><creatorcontrib>Kallies, Axel</creatorcontrib><creatorcontrib>Heikenwalder, Mathias</creatorcontrib><creatorcontrib>Heissmeyer, Vigo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Nature immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jeltsch, Katharina M</au><au>Hu, Desheng</au><au>Brenner, Sven</au><au>Zöller, Jessica</au><au>Heinz, Gitta A</au><au>Nagel, Daniel</au><au>Vogel, Katharina U</au><au>Rehage, Nina</au><au>Warth, Sebastian C</au><au>Edelmann, Stephanie L</au><au>Gloury, Renee</au><au>Martin, Nina</au><au>Lohs, Claudia</au><au>Lech, Maciej</au><au>Stehklein, Jenny E</au><au>Geerlof, Arie</au><au>Kremmer, Elisabeth</au><au>Weber, Achim</au><au>Anders, Hans-Joachim</au><au>Schmitz, Ingo</au><au>Schmidt-Supprian, Marc</au><au>Fu, Mingui</au><au>Holtmann, Helmut</au><au>Krappmann, Daniel</au><au>Ruland, Jürgen</au><au>Kallies, Axel</au><au>Heikenwalder, Mathias</au><au>Heissmeyer, Vigo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation</atitle><jtitle>Nature immunology</jtitle><addtitle>Nat Immunol</addtitle><date>2014-11</date><risdate>2014</risdate><volume>15</volume><issue>11</issue><spage>1079</spage><pages>1079-</pages><eissn>1529-2916</eissn><abstract>Humoral autoimmunity paralleled by the accumulation of follicular helper T cells (T(FH) cells) is linked to mutation of the gene encoding the RNA-binding protein roquin-1. Here we found that T cells lacking roquin caused pathology in the lung and accumulated as cells of the T(H)17 subset of helper T cells in the lungs. Roquin inhibited T(H)17 cell differentiation and acted together with the endoribonuclease regnase-1 to repress target mRNA encoding the T(H)17 cell-promoting factors IL-6, ICOS, c-Rel, IRF4, IκBNS and IκBζ. This cooperation required binding of RNA by roquin and the nuclease activity of regnase-1. Upon recognition of antigen by the T cell antigen receptor (TCR), roquin and regnase-1 proteins were cleaved by the paracaspase MALT1. Thus, this pathway acts as a 'rheostat' by translating TCR signal strength via graded inactivation of post-transcriptional repressors and differential derepression of targets to enhance T(H)17 differentiation.</abstract><cop>United States</cop><pmid>25282160</pmid><doi>10.1038/ni.3008</doi><orcidid>https://orcid.org/0000000157713907</orcidid><orcidid>https://orcid.org/0000000253600419</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | EISSN: 1529-2916 |
| ispartof | Nature immunology, 2014-11, Vol.15 (11), p.1079 |
| issn | 1529-2916 |
| language | eng |
| recordid | cdi_pubmed_primary_25282160 |
| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature |
| subjects | Adaptor Proteins, Signal Transducing - genetics Amino Acid Sequence Animals Binding Sites - immunology Caspases - metabolism Cell Differentiation - immunology Cell Line Genes, rel - genetics HEK293 Cells Humans Inducible T-Cell Co-Stimulator Protein - genetics Interferon Regulatory Factors - genetics Interleukin-6 - genetics Intracellular Signaling Peptides and Proteins Lung - immunology Lung - pathology Mice Mice, Inbred BALB C Mice, Inbred C57BL Mice, Inbred NOD Mice, Knockout Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein Neoplasm Proteins - metabolism Nuclear Proteins - genetics Proteins - genetics Receptors, Antigen, T-Cell - immunology Ribonucleases - metabolism RNA, Messenger - genetics RNA-Binding Proteins - metabolism Sequence Alignment Th17 Cells - cytology Th17 Cells - immunology Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism |
| title | Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T20%3A48%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cleavage%20of%20roquin%20and%20regnase-1%20by%20the%20paracaspase%20MALT1%20releases%20their%20cooperatively%20repressed%20targets%20to%20promote%20T(H)17%20differentiation&rft.jtitle=Nature%20immunology&rft.au=Jeltsch,%20Katharina%20M&rft.date=2014-11&rft.volume=15&rft.issue=11&rft.spage=1079&rft.pages=1079-&rft.eissn=1529-2916&rft_id=info:doi/10.1038/ni.3008&rft_dat=%3Cpubmed%3E25282160%3C/pubmed%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/25282160&rfr_iscdi=true |