Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins.

Détails

ID Serval
serval:BIB_5CA727BDC360
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins.
Périodique
Biochemical and Biophysical Research Communications
Auteur(s)
Ciano M., Allocca S., Ciardulli M.C., Della Volpe L., Bonatti S., D'Agostino M.
ISSN
1090-2104 (Electronic)
ISSN-L
0006-291X
Statut éditorial
Publié
Date de publication
2016
Peer-reviewed
Oui
Volume
479
Numéro
2
Pages
325-330
Langue
anglais
Résumé
We have previously shown that αB-crystallin (CRYAB), a small heat shock protein (sHsp) that prevents irreversible aggregation of unfolded protein by an ATP-independent chaperone activity, plays a pivotal role in the biogenesis of multipass transmembrane proteins (TMPs) assisting their folding from the cytosolic side of the endoplasmic reticulum (ER) (D'Agostino et al., 2013). Here we present evidence, based on phosphomimetic substitutions, that the three phosphorytable serine residues at position 19, 45 and 59 of CRYAB play a different regulatory role in this novel chaperone activity: S19 and S45 have a strong inhibitory effect, either alone or in combination, while S59 has not and counteracts the inhibition caused by single phosphomimetic substitutions at S19 and S45. Interestingly, all phosphomimetic substitutions determine the formation of smaller oligomeric complexes containing CRYAB, indicating that the inhibitory effect seen for S19 and S45 cannot be ascribed to the reduction of oligomerization frequently associated to a decreased chaperone activity. These results indicate that phosphorylation finely regulates the chaperone activity of CRYAB with multipass TMPs and suggest a pivotal role for S59 in this process.
Mots-clé
Spectral graph theory, filter design, tight frames, signal processing on graphs
Pubmed
Web of science
Open Access
Oui
Création de la notice
10/11/2016 13:55
Dernière modification de la notice
20/08/2019 15:15
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