The components of the AhR-molecular chaperone complex differ depending on whether the ligands are toxic or non-toxic.
FEBS Lett
; 598(12): 1478-1490, 2024 Jun.
Article
em En
| MEDLINE
| ID: mdl-38605276
ABSTRACT
The aryl hydrocarbon receptor (AhR) forms a complex with the HSP90-XAP2-p23 molecular chaperone when the cells are exposed to toxic compounds. Recently, 1,4-dihydroxy-2-naphthoic acid (DHNA) was reported to be an AhR ligand. Here, we investigated the components of the molecular chaperone complex when DHNA binds to AhR. Proteins eluted from the 3-Methylcolanthrene-affinity column were AhR-HSP90-XAP2-p23 complex. The AhR-molecular chaperone complex did not contain p23 in the eluents from the DHNA-affinity column. In 3-MC-treated cells, AhR formed a complex with HSP90-XAP2-p23 and nuclear translocation occurred within 30 min, while in DHNA-treated cells, AhR formed a complex with AhR-HSP90-XAP2, and translocation was slow from 60 min. Thus, the AhR activation mechanism may differ when DHNA is the ligand compared to toxic ligands.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Receptores de Hidrocarboneto Arílico
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Proteínas de Choque Térmico HSP90
Limite:
Animals
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Humans
Idioma:
En
Revista:
FEBS Lett
/
FEBS lett
/
Febs letters
Ano de publicação:
2024
Tipo de documento:
Article