Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta
DC Element | Wert | Sprache |
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dc.contributor.author | Fan, Lu | |
dc.contributor.author | Kishore, Anusha | |
dc.contributor.author | Jansen-Olliges, Linda | |
dc.contributor.author | Wang, Dahua | |
dc.contributor.author | Stahl, Frank | |
dc.contributor.author | Psathaki, Olympia Ekaterini | |
dc.contributor.author | Harre, Jennifer | |
dc.contributor.author | Warnecke, Athanasia | |
dc.contributor.author | Weder, Julia | |
dc.contributor.author | Preller, Matthias | |
dc.contributor.author | Zeilinger, Carsten | |
dc.date.accessioned | 2023-02-17T11:36:18Z | - |
dc.date.available | 2023-02-17T11:36:18Z | - |
dc.date.issued | 2022 | |
dc.identifier.issn | 2470-1343 | |
dc.identifier.uri | http://osnascholar.ub.uni-osnabrueck.de/handle/unios/65566 | - |
dc.description.abstract | While many proteins are known clients of heat shock protein 90 (Hsp90), it is unclear whether the transcription factor, thyroid hormone receptor beta (TRb), interacts with Hsp90 to control hormonal perception and signaling. Higher Hsp90 expression in mouse fibroblasts was elicited by the addition of triiodothyronine (T3). T3 bound to Hsp90 and enhanced adenosine triphosphate (ATP) binding of Hsp90 due to a specific binding site for T3, as identified by molecular docking experiments. The binding of TRb to Hsp90 was prevented by T3 or by the thyroid mimetic sobetirome. Purified recombinant TRb trapped Hsp90 from cell lysate or purified Hsp90 in pull-down experiments. The affinity of Hsp90 for TRb was 124 nM. Furthermore, T3 induced the release of bound TRb from Hsp90, which was shown by streptavidin-conjugated quantum dot (SAv-QD) masking assay. The data indicate that the T3 interaction with TRb and Hsp90 may be an amplifier of the cellular stress response by blocking Hsp90 activity. | |
dc.description.sponsorship | Bundesinstitut fur Sportwissenschaft (BISP) [ZMVI4-070514/ 20-21]; DFG; [CSC201706180024]; [CSC202008080018]; L.F. and D.W. were financed by CSC201706180024 and CSC202008080018, respectively; A.K. was funded by the Bundesinstitut fur Sportwissenschaft (BISP, ZMVI4-070514/ 20-21) and E.P. by the DFG SFB 944 Z-Project. The DFG FOR Cytolabs also supported consumables, Excellence Cluster Rebirth Innovation-/Synergy Grants Screening of Telomerase Stimulators for Cardiac Regeneration & Repair (CR&R) by Cell Microarrays and the Cluster of Excellence Hearing4All (EXC 2177/1). | |
dc.language.iso | en | |
dc.publisher | AMER CHEMICAL SOC | |
dc.relation.ispartof | ACS OMEGA | |
dc.subject | ACTIVATION | |
dc.subject | Chemistry | |
dc.subject | Chemistry, Multidisciplinary | |
dc.subject | EXPRESSION | |
dc.subject | GENES | |
dc.subject | GLUCOCORTICOID-RECEPTOR | |
dc.subject | HEAT-SHOCK-PROTEIN | |
dc.subject | HSP70 | |
dc.subject | LOCALIZATION | |
dc.subject | MECHANISMS | |
dc.subject | MORPHOLOGY | |
dc.subject | MUTANTS | |
dc.title | Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta | |
dc.type | journal article | |
dc.identifier.doi | 10.1021/acsomega.2c02331 | |
dc.identifier.isi | ISI:000840799200001 | |
dc.description.volume | 7 | |
dc.description.issue | 33 | |
dc.description.startpage | 28932 | |
dc.description.endpage | 28945 | |
dc.contributor.researcherid | HHC-6174-2022 | |
dc.publisher.place | 1155 16TH ST, NW, WASHINGTON, DC 20036 USA | |
dcterms.isPartOf.abbreviation | ACS Omega | |
dcterms.oaStatus | Green Published | |
local.import.remains | affiliations : Leibniz University Hannover; Hannover Medical School; Leibniz University Hannover; University Osnabruck; Hannover Medical School; Hochschule Bonn Rhein Sieg | |
local.import.remains | earlyaccessdate : AUG 2022 | |
local.import.remains | web-of-science-index : Science Citation Index Expanded (SCI-EXPANDED) | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0002-4035-6840 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | PsOl764 | - |
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geprüft am 09.06.2024