The ‘PINIT’ motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L
PIAS proteins, cytokine-dependent STAT-associated repressors, exhibit intrinsic E3-type SUMO ligase activities and form a family of transcriptional modulators. Three conserved domains have been identified so far in this protein family, the SAP box, the MIZ-Zn finger/RING module and the acidic C-term...
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| Veröffentlicht in: | FEBS letters 2003-11, Vol.554 (1-2), p.111-118 |
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| container_title | FEBS letters |
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| creator | Duval, D. Duval, G. Kedinger, C. Poch, O. Boeuf, H. |
| description | PIAS proteins, cytokine-dependent STAT-associated repressors, exhibit intrinsic E3-type SUMO ligase activities and form a family of transcriptional modulators. Three conserved domains have been identified so far in this protein family, the SAP box, the MIZ-Zn finger/RING module and the acidic C-terminal domain, which are essential for protein interactions, DNA binding or SUMO ligase activity. We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its ‘PINIT’ motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L, the long form of PIAS3, that we have characterized in mouse embryonic stem cells. |
| doi_str_mv | 10.1016/S0014-5793(03)01116-5 |
| format | Article |
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Three conserved domains have been identified so far in this protein family, the SAP box, the MIZ-Zn finger/RING module and the acidic C-terminal domain, which are essential for protein interactions, DNA binding or SUMO ligase activity. We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its ‘PINIT’ motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L, the long form of PIAS3, that we have characterized in mouse embryonic stem cells.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(03)01116-5</identifier><identifier>PMID: 14596924</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Active Transport, Cell Nucleus ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biochemistry, Molecular Biology ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Line ; Cloning, Molecular ; Conserved Sequence ; DNA, Complementary ; E3-type SUMO ligase ; Embryonic stem cell ; ES, embryonic stem ; Gene Expression Regulation ; Genetic Variation ; Intracellular Signaling Peptides and Proteins ; LIF, leukemia inhibitory factor ; Life Sciences ; Mice ; Molecular Sequence Data ; Nuclear localization ; PIAS ; PIAS, protein inhibitor of activated STATs ; Protein Inhibitors of Activated STAT ; Protein Structure, Tertiary ; SAP, Saf-A/B, Acinus and Pias ; Sequence Alignment ; STAT repressor ; STAT, signal transducer and activator of transcription ; SUMO, small ubiquitin-related modifier</subject><ispartof>FEBS letters, 2003-11, Vol.554 (1-2), p.111-118</ispartof><rights>2003 Federation of European Biochemical Societies</rights><rights>FEBS Letters 554 (2003) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6255-803480224e60414cc21b01b08da7ae88a05b671e0cf5a80c1b883817355f35833</citedby><cites>FETCH-LOGICAL-c6255-803480224e60414cc21b01b08da7ae88a05b671e0cf5a80c1b883817355f35833</cites><orcidid>0000-0002-7134-3217</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2803%2901116-5$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(03)01116-5$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14596924$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04145145$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Duval, D.</creatorcontrib><creatorcontrib>Duval, G.</creatorcontrib><creatorcontrib>Kedinger, C.</creatorcontrib><creatorcontrib>Poch, O.</creatorcontrib><creatorcontrib>Boeuf, H.</creatorcontrib><title>The ‘PINIT’ motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>PIAS proteins, cytokine-dependent STAT-associated repressors, exhibit intrinsic E3-type SUMO ligase activities and form a family of transcriptional modulators. Three conserved domains have been identified so far in this protein family, the SAP box, the MIZ-Zn finger/RING module and the acidic C-terminal domain, which are essential for protein interactions, DNA binding or SUMO ligase activity. We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its ‘PINIT’ motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L, the long form of PIAS3, that we have characterized in mouse embryonic stem cells.</description><subject>Active Transport, Cell Nucleus</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biochemistry, Molecular Biology</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>Conserved Sequence</subject><subject>DNA, Complementary</subject><subject>E3-type SUMO ligase</subject><subject>Embryonic stem cell</subject><subject>ES, embryonic stem</subject><subject>Gene Expression Regulation</subject><subject>Genetic Variation</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>LIF, leukemia inhibitory factor</subject><subject>Life Sciences</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Nuclear localization</subject><subject>PIAS</subject><subject>PIAS, protein inhibitor of activated STATs</subject><subject>Protein Inhibitors of Activated STAT</subject><subject>Protein Structure, Tertiary</subject><subject>SAP, Saf-A/B, Acinus and Pias</subject><subject>Sequence Alignment</subject><subject>STAT repressor</subject><subject>STAT, signal transducer and activator of transcription</subject><subject>SUMO, small ubiquitin-related modifier</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUcFuEzEUtBCIhsIngHxCVOqCvbZ3nRMKVUsiRVCp4Ww53reqkXdd7E2q3HrqN5Tf65dgZ6NyBOlJtufNzLM9CL2l5CMltPp0RQjlhain7ANhJ4RSWhXiGZpQWbOC8Uo-R5MnyhF6FeNPks6STl-iI8rFtJqWfILuV9eAH-8eLhffFqvHu9-484NtT7FvscY93Lodtg30CbPQYOP7CGGbdo3vtO0zbUgGl4vZFb4JfoCEtbqzbneKbcQQY9Zqh1sfcL8xDnTAAYaM-r08S9nyNXrRahfhzWE9Rj8uzldn82L5_evibLYsTFUKUUjCuCRlyaEinHJjSromqWSjaw1SaiLWVU2BmFZoSQxdS8kkrZkQLROSsWN0Mvpea6dugu102CmvrZrPlipj2Vak2tLEfT9y08N-bSAOqrPRgHO6B7-JqqaM1VyQRBQj0QQfY4D2yZkSlcNS-7BUTkKRVDksJZLu3WHAZt1B81d1SCcR5iPh1jrY_Z-rujj_Uu47uUHYHs6zPo9WkH53ayGoaCz0BhobwAyq8fYft_0D9hu2rw</recordid><startdate>20031106</startdate><enddate>20031106</enddate><creator>Duval, D.</creator><creator>Duval, G.</creator><creator>Kedinger, C.</creator><creator>Poch, O.</creator><creator>Boeuf, H.</creator><general>Elsevier B.V</general><general>Wiley</general><scope>6I.</scope><scope>AAFTH</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>1XC</scope><orcidid>https://orcid.org/0000-0002-7134-3217</orcidid></search><sort><creationdate>20031106</creationdate><title>The ‘PINIT’ motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L</title><author>Duval, D. ; Duval, G. ; Kedinger, C. ; Poch, O. ; Boeuf, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6255-803480224e60414cc21b01b08da7ae88a05b671e0cf5a80c1b883817355f35833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Active Transport, Cell Nucleus</topic><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biochemistry, Molecular Biology</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>Conserved Sequence</topic><topic>DNA, Complementary</topic><topic>E3-type SUMO ligase</topic><topic>Embryonic stem cell</topic><topic>ES, embryonic stem</topic><topic>Gene Expression Regulation</topic><topic>Genetic Variation</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>LIF, leukemia inhibitory factor</topic><topic>Life Sciences</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Nuclear localization</topic><topic>PIAS</topic><topic>PIAS, protein inhibitor of activated STATs</topic><topic>Protein Inhibitors of Activated STAT</topic><topic>Protein Structure, Tertiary</topic><topic>SAP, Saf-A/B, Acinus and Pias</topic><topic>Sequence Alignment</topic><topic>STAT repressor</topic><topic>STAT, signal transducer and activator of transcription</topic><topic>SUMO, small ubiquitin-related modifier</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Duval, D.</creatorcontrib><creatorcontrib>Duval, G.</creatorcontrib><creatorcontrib>Kedinger, C.</creatorcontrib><creatorcontrib>Poch, O.</creatorcontrib><creatorcontrib>Boeuf, H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Hyper Article en Ligne (HAL)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Duval, D.</au><au>Duval, G.</au><au>Kedinger, C.</au><au>Poch, O.</au><au>Boeuf, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ‘PINIT’ motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2003-11-06</date><risdate>2003</risdate><volume>554</volume><issue>1-2</issue><spage>111</spage><epage>118</epage><pages>111-118</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>PIAS proteins, cytokine-dependent STAT-associated repressors, exhibit intrinsic E3-type SUMO ligase activities and form a family of transcriptional modulators. Three conserved domains have been identified so far in this protein family, the SAP box, the MIZ-Zn finger/RING module and the acidic C-terminal domain, which are essential for protein interactions, DNA binding or SUMO ligase activity. We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its ‘PINIT’ motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L, the long form of PIAS3, that we have characterized in mouse embryonic stem cells.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>14596924</pmid><doi>10.1016/S0014-5793(03)01116-5</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-7134-3217</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 2003-11, Vol.554 (1-2), p.111-118 |
| issn | 0014-5793 1873-3468 |
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| source | MEDLINE; Access via Wiley Online Library; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); Alma/SFX Local Collection |
| subjects | Active Transport, Cell Nucleus Amino Acid Motifs Amino Acid Sequence Animals Biochemistry, Molecular Biology Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cell Line Cloning, Molecular Conserved Sequence DNA, Complementary E3-type SUMO ligase Embryonic stem cell ES, embryonic stem Gene Expression Regulation Genetic Variation Intracellular Signaling Peptides and Proteins LIF, leukemia inhibitory factor Life Sciences Mice Molecular Sequence Data Nuclear localization PIAS PIAS, protein inhibitor of activated STATs Protein Inhibitors of Activated STAT Protein Structure, Tertiary SAP, Saf-A/B, Acinus and Pias Sequence Alignment STAT repressor STAT, signal transducer and activator of transcription SUMO, small ubiquitin-related modifier |
| title | The ‘PINIT’ motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L |
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