Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Lu Fan
  • Anusha Kishore
  • Linda Jansen-Olliges
  • Dahua Wang
  • Frank Stahl
  • Olympia Ekaterini Psathaki
  • Jennifer Harre
  • Athanasia Warnecke
  • Julia Weder
  • Matthias Preller
  • Carsten Zeilinger

Externe Organisationen

  • Medizinische Hochschule Hannover (MHH)
  • Universität Osnabrück
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)28932-28945
Seitenumfang14
FachzeitschriftACS Omega
Jahrgang7
Ausgabenummer33
Frühes Online-Datum9 Aug. 2022
PublikationsstatusVeröffentlicht - 23 Aug. 2022

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.

ASJC Scopus Sachgebiete

Zitieren

Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta. / Fan, Lu; Kishore, Anusha; Jansen-Olliges, Linda et al.
in: ACS Omega, Jahrgang 7, Nr. 33, 23.08.2022, S. 28932-28945.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Fan, L, Kishore, A, Jansen-Olliges, L, Wang, D, Stahl, F, Psathaki, OE, Harre, J, Warnecke, A, Weder, J, Preller, M & Zeilinger, C 2022, 'Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta', ACS Omega, Jg. 7, Nr. 33, S. 28932-28945. https://doi.org/10.1021/acsomega.2c02331
Fan, L., Kishore, A., Jansen-Olliges, L., Wang, D., Stahl, F., Psathaki, O. E., Harre, J., Warnecke, A., Weder, J., Preller, M., & Zeilinger, C. (2022). Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta. ACS Omega, 7(33), 28932-28945. https://doi.org/10.1021/acsomega.2c02331
Fan L, Kishore A, Jansen-Olliges L, Wang D, Stahl F, Psathaki OE et al. Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta. ACS Omega. 2022 Aug 23;7(33):28932-28945. Epub 2022 Aug 9. doi: 10.1021/acsomega.2c02331
Fan, Lu ; Kishore, Anusha ; Jansen-Olliges, Linda et al. / Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta. in: ACS Omega. 2022 ; Jahrgang 7, Nr. 33. S. 28932-28945.
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title = "Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta",
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.",
author = "Lu Fan and Anusha Kishore and Linda Jansen-Olliges and Dahua Wang and Frank Stahl and Psathaki, {Olympia Ekaterini} and Jennifer Harre and Athanasia Warnecke and Julia Weder and Matthias Preller and Carsten Zeilinger",
note = "Funding Information: L.F. and D.W. were financed by CSC201706180024 and CSC202008080018, respectively; A.K. was funded by the Bundesinstitut f{\"u}r 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).",
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AU - Fan, Lu

AU - Kishore, Anusha

AU - Jansen-Olliges, Linda

AU - Wang, Dahua

AU - Stahl, Frank

AU - Psathaki, Olympia Ekaterini

AU - Harre, Jennifer

AU - Warnecke, Athanasia

AU - Weder, Julia

AU - Preller, Matthias

AU - Zeilinger, Carsten

N1 - Funding Information: L.F. and D.W. were financed by CSC201706180024 and CSC202008080018, respectively; A.K. was funded by the Bundesinstitut für 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).

PY - 2022/8/23

Y1 - 2022/8/23

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.

AB - 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.

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JO - ACS Omega

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