Phenylalanine hydroxylase variants interact with the co-chaperone DNAJC12.
HSP40 co-chaperones
hyperphenylalanine
molecular chaperones
protein aggregation
protein misfolding
Journal
Human mutation
ISSN: 1098-1004
Titre abrégé: Hum Mutat
Pays: United States
ID NLM: 9215429
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
07
11
2018
revised:
12
01
2019
accepted:
19
01
2019
pubmed:
23
1
2019
medline:
12
3
2020
entrez:
23
1
2019
Statut:
ppublish
Résumé
DNAJC12, a type III member of the HSP40/DNAJ family, has been identified as the specific co-chaperone of phenylalanine hydroxylase (PAH) and the other aromatic amino acid hydroxylases. DNAJ proteins work together with molecular chaperones of the HSP70 family to assist in proper folding and maintenance of intracellular stability of their clients. Autosomal recessive mutations in DNAJC12 were found to reduce PAH levels, leading to hyperphenylalaninemia (HPA) in patients without mutations in PAH. In this work, we investigated the interaction of normal wild-type DNAJC12 with mutant PAH in cells expressing several PAH variants associated with HPA in humans, as well as in the Enu
Substances chimiques
Biomarkers
0
DNAJC12 protein, human
0
Molecular Chaperones
0
Repressor Proteins
0
Phenylalanine Hydroxylase
EC 1.14.16.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
483-494Subventions
Organisme : Research Council of Norway
ID : FRIMEDBIO 261826/F20
Pays : International
Organisme : Research Council of Norway
ID : FORNY 248889/O30
Pays : International
Organisme : K.G. Jebsen Centre for Neuropsychiatric Disorders
Pays : International
Organisme : the Western Norway Regional Health Authorities
ID : 912246
Pays : International
Organisme : European Commission
ID : FP7-HEALTH-2012-INNOVATION-1 EU
Pays : International
Organisme : European Commission
ID : 305444
Pays : International
Informations de copyright
© 2019 Wiley Periodicals, Inc.