Geiger, Thomas M. ; Hähle, Andreas ; Merz, Stephanie ; Meyners, Christian ; Tianqi, Mao ; Kolos, Jürgen ; Hausch, Felix (2019)
FKBP51 and FKBP12.6—Novel and tight interactors of Glomulin.
In: PLOS ONE, 14 (9)
doi: 10.1371/journal.pone.0221926
Artikel, Bibliographie
Dies ist die neueste Version dieses Eintrags.
Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2019 |
| Autor(en): | Geiger, Thomas M. ; Hähle, Andreas ; Merz, Stephanie ; Meyners, Christian ; Tianqi, Mao ; Kolos, Jürgen ; Hausch, Felix |
| Art des Eintrags: | Bibliographie |
| Titel: | FKBP51 and FKBP12.6—Novel and tight interactors of Glomulin |
| Sprache: | Englisch |
| Publikationsjahr: | 2019 |
| Verlag: | PLOS |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | PLOS ONE |
| Jahrgang/Volume einer Zeitschrift: | 14 |
| (Heft-)Nummer: | 9 |
| DOI: | 10.1371/journal.pone.0221926 |
| URL / URN: | https://doi.org/10.1371/journal.pone.0221926 |
| Zugehörige Links: | |
| Kurzbeschreibung (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. |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 540 Chemie |
| Fachbereich(e)/-gebiet(e): | 07 Fachbereich Chemie 07 Fachbereich Chemie > Clemens-Schöpf-Institut > Fachgebiet Biochemie 07 Fachbereich Chemie > Clemens-Schöpf-Institut |
| Hinterlegungsdatum: | 02 Aug 2024 12:34 |
| Letzte Änderung: | 02 Aug 2024 12:34 |
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| Suche nach Titel in: | TUfind oder in Google |
Verfügbare Versionen dieses Eintrags
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FKBP51 and FKBP12.6—Novel and tight interactors of Glomulin. (deposited 03 Nov 2019 20:57)
- FKBP51 and FKBP12.6—Novel and tight interactors of Glomulin. (deposited 02 Aug 2024 12:34) [Gegenwärtig angezeigt]
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