TU Darmstadt / ULB / TUprints

FKBP51 and FKBP12.6—Novel and tight interactors of Glomulin

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), PLOS, ISSN 1932-6203,

Copyright Information: CC BY 4.0 International - Creative Commons, Attribution.

Download (1MB) | Preview
Item Type: Article
Origin: Secondary publication via sponsored Golden Open Access
Title: FKBP51 and FKBP12.6—Novel and tight interactors of Glomulin
Language: English

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.

Journal or Publication Title: PLOS ONE
Volume of the journal: 14
Issue Number: 9
Place of Publication: Darmstadt
Publisher: PLOS
Classification DDC: 500 Naturwissenschaften und Mathematik > 540 Chemie
Divisions: 07 Department of Chemistry > Fachgebiet Biochemie
Date Deposited: 29 Oct 2019 08:33
Last Modified: 13 Dec 2022 10:48
Corresponding Links:
URN: urn:nbn:de:tuda-tuprints-92111
URI: https://tuprints.ulb.tu-darmstadt.de/id/eprint/9211
Actions (login required)
View Item View Item