FKBP51 and FKBP12.6-Novel and tight interactors of Glomulin
The protein factor Glomulin (Glmn) is a regulator of the SCF (Skp1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Mutations of Glmn lead to glomuvenous malformations. Glmn has been reported to be associated with FK506-binding proteins (FKBP). Here we present in vitro binding analyses of th...
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| creator | Hähle, Andreas Geiger, Thomas M Merz, Stephanie Meyners, Christian Tianqi, Mao Kolos, Jürgen Hausch, Felix |
| description | The protein factor Glomulin (Glmn) is a regulator of the SCF (Skp1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Mutations of Glmn lead to glomuvenous malformations. Glmn has been reported to be associated with FK506-binding proteins (FKBP). Here we present in vitro binding analyses of the FKBP-Glmn interaction. Interestingly, the previously described interaction of Glmn and FKBP12 was found to be comparatively weak. Instead, the closely related FKBP12.6 and FKBP51 emerged as novel binding partners. We show different binding affinities of full length and truncated FKBP51 and FKBP52 mutants. Using FKBP51 as a model system, we show that two amino acids lining the FK506-binding site are essential for binding Glmn and that the FKBP51-Glmn interaction is blocked by FKBP ligands. This data suggest FKBP inhibition as a pharmacological approach to regulate Glmn and Glmn-controlled processes. |
| doi_str_mv | 10.1371/journal.pone.0221926 |
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Mutations of Glmn lead to glomuvenous malformations. Glmn has been reported to be associated with FK506-binding proteins (FKBP). Here we present in vitro binding analyses of the FKBP-Glmn interaction. Interestingly, the previously described interaction of Glmn and FKBP12 was found to be comparatively weak. Instead, the closely related FKBP12.6 and FKBP51 emerged as novel binding partners. We show different binding affinities of full length and truncated FKBP51 and FKBP52 mutants. Using FKBP51 as a model system, we show that two amino acids lining the FK506-binding site are essential for binding Glmn and that the FKBP51-Glmn interaction is blocked by FKBP ligands. This data suggest FKBP inhibition as a pharmacological approach to regulate Glmn and Glmn-controlled processes.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0221926</identifier><identifier>PMID: 31490997</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Amino acids ; Apoptosis ; Binding proteins ; Binding sites ; Biochemistry ; Biology and Life Sciences ; Catalytic Domain ; F-box protein ; Gene expression ; Ligands ; Ligases ; Metabolism ; Mutants ; Mutation ; Novels ; Organic chemistry ; Physical Sciences ; Protein Binding ; Proteins ; Research and Analysis Methods ; Tacrolimus ; Tacrolimus Binding Proteins - chemistry ; Tacrolimus Binding Proteins - genetics ; Tacrolimus Binding Proteins - metabolism ; Tacrolimus-binding protein ; Ubiquitin ; Ubiquitin-protein ligase</subject><ispartof>PloS one, 2019-09, Vol.14 (9), p.e0221926-e0221926</ispartof><rights>COPYRIGHT 2019 Public Library of Science</rights><rights>2019 Hähle et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 Hähle et al 2019 Hähle et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-d8144db4c9f2ba963d6be927a9e37f6b7bfe071a85a7abd2f19db0911fdcd91c3</citedby><cites>FETCH-LOGICAL-c692t-d8144db4c9f2ba963d6be927a9e37f6b7bfe071a85a7abd2f19db0911fdcd91c3</cites><orcidid>0000-0002-3710-8838</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6730887/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6730887/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,866,887,2106,2932,23875,27933,27934,53800,53802</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31490997$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Picard, Didier</contributor><creatorcontrib>Hähle, Andreas</creatorcontrib><creatorcontrib>Geiger, Thomas M</creatorcontrib><creatorcontrib>Merz, Stephanie</creatorcontrib><creatorcontrib>Meyners, Christian</creatorcontrib><creatorcontrib>Tianqi, Mao</creatorcontrib><creatorcontrib>Kolos, Jürgen</creatorcontrib><creatorcontrib>Hausch, Felix</creatorcontrib><title>FKBP51 and FKBP12.6-Novel and tight interactors of Glomulin</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The protein factor Glomulin (Glmn) is a regulator of the SCF (Skp1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Mutations of Glmn lead to glomuvenous malformations. Glmn has been reported to be associated with FK506-binding proteins (FKBP). Here we present in vitro binding analyses of the FKBP-Glmn interaction. Interestingly, the previously described interaction of Glmn and FKBP12 was found to be comparatively weak. Instead, the closely related FKBP12.6 and FKBP51 emerged as novel binding partners. We show different binding affinities of full length and truncated FKBP51 and FKBP52 mutants. Using FKBP51 as a model system, we show that two amino acids lining the FK506-binding site are essential for binding Glmn and that the FKBP51-Glmn interaction is blocked by FKBP ligands. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hähle, Andreas</au><au>Geiger, Thomas M</au><au>Merz, Stephanie</au><au>Meyners, Christian</au><au>Tianqi, Mao</au><au>Kolos, Jürgen</au><au>Hausch, Felix</au><au>Picard, Didier</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FKBP51 and FKBP12.6-Novel and tight interactors of Glomulin</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2019-09-06</date><risdate>2019</risdate><volume>14</volume><issue>9</issue><spage>e0221926</spage><epage>e0221926</epage><pages>e0221926-e0221926</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The protein factor Glomulin (Glmn) is a regulator of the SCF (Skp1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Mutations of Glmn lead to glomuvenous malformations. Glmn has been reported to be associated with FK506-binding proteins (FKBP). Here we present in vitro binding analyses of the FKBP-Glmn interaction. Interestingly, the previously described interaction of Glmn and FKBP12 was found to be comparatively weak. Instead, the closely related FKBP12.6 and FKBP51 emerged as novel binding partners. We show different binding affinities of full length and truncated FKBP51 and FKBP52 mutants. Using FKBP51 as a model system, we show that two amino acids lining the FK506-binding site are essential for binding Glmn and that the FKBP51-Glmn interaction is blocked by FKBP ligands. This data suggest FKBP inhibition as a pharmacological approach to regulate Glmn and Glmn-controlled processes.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>31490997</pmid><doi>10.1371/journal.pone.0221926</doi><tpages>e0221926</tpages><orcidid>https://orcid.org/0000-0002-3710-8838</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - metabolism Amino acids Apoptosis Binding proteins Binding sites Biochemistry Biology and Life Sciences Catalytic Domain F-box protein Gene expression Ligands Ligases Metabolism Mutants Mutation Novels Organic chemistry Physical Sciences Protein Binding Proteins Research and Analysis Methods Tacrolimus Tacrolimus Binding Proteins - chemistry Tacrolimus Binding Proteins - genetics Tacrolimus Binding Proteins - metabolism Tacrolimus-binding protein Ubiquitin Ubiquitin-protein ligase |
| title | FKBP51 and FKBP12.6-Novel and tight interactors of Glomulin |
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