Mutations F352A and Y528A in human HSP90α reduce fibronectin association and fibrillogenesis in cell-derived matrices.
Extracellular matrix
Fibronectin
Hsp90
Mutagenesis
Journal
Cell stress & chaperones
ISSN: 1466-1268
Titre abrégé: Cell Stress Chaperones
Pays: Netherlands
ID NLM: 9610925
Informations de publication
Date de publication:
23 Jun 2023
23 Jun 2023
Historique:
received:
13
03
2023
accepted:
09
06
2023
revised:
29
05
2023
medline:
24
6
2023
pubmed:
24
6
2023
entrez:
23
6
2023
Statut:
aheadofprint
Résumé
HSP90 is a ubiquitously expressed chaperone protein that regulates the maturation of numerous substrate proteins called 'clients'. The glycoprotein fibronectin (FN) is an important protein of the extracellular matrix (ECM) and a client protein of HSP90. FN and HSP90 interact directly, and the FN ECM is regulated by exogenous HSP90 or HSP90 inhibitors. Here, we extend the analysis of the HSP90 - FN interaction. The importance of the N-terminal 70-kDa fragment of fibronectin (FN70) and FN type I repeat was demonstrated by competition for FN binding between HSP90 and the functional upstream domain (FUD) of the Streptococcus pyogenes F1 adhesin protein. Furthermore, His-HSP90α mutations F352A and Y528A (alone and in combination) reduced the association with full-length FN (FN-FL) and FN70 in vitro. Unlike wild type His-HSP90α, these HSP90 mutants did not enhance FN matrix assembly in the Hs578T cell line model when added exogenously. Interestingly, the HSP90 E353A mutation, which did not significantly reduce the HSP90 - FN interaction in vitro, dramatically blocked FN matrix assembly in Hs578T cell-derived matrices. Taken together, these data extend our understanding of the role of HSP90 in FN fibrillogenesis and suggest that promotion of FN ECM assembly by HSP90 is not solely regulated by the affinity of the direct interaction between HSP90 and FN.
Identifiants
pubmed: 37353709
doi: 10.1007/s12192-023-01362-9
pii: 10.1007/s12192-023-01362-9
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : National Research Foundation
ID : 98566
Organisme : National Research Foundation
ID : 129262
Organisme : National Research Foundation
ID : SARChI Postdoctoral Fellowship
Organisme : Deutscher Akademischer Austauschdienst
ID : In Region PhD Fellowship
Organisme : Rhodes University
ID : RGG
Informations de copyright
© 2023. The Author(s).
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