TY  - JOUR
U1  - Zeitschriftenartikel, wissenschaftlich - begutachtet (reviewed)
A1  - Fan, Lu
A1  - Kishore, Anusha
A1  - Jansen-Olliges, Linda
A1  - Wang, Dahua
A1  - Stahl, Frank
A1  - Psathaki, Olympia Ekaterini
A1  - Harre, Jennifer
A1  - Warnecke, Athanasia
A1  - Weder, Julia
A1  - Preller, Matthias
A1  - Zeilinger, Carsten
T1  - Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta
JF  - ACS Omega
N2  - 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.
UN  - https://nbn-resolving.org/urn:nbn:de:hbz:1044-opus-64102
SN  - 2470-1343
SS  - 2470-1343
U6  - https://doi.org/10.1021/acsomega.2c02331
DO  - https://doi.org/10.1021/acsomega.2c02331
PM  - 36033668
VL  - 7
IS  - 33
SP  - 28932
EP  - 28945
S1  - 14
PB  - American Chemical Society (ACS)
ER  -