MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP.
Adenosine Triphosphate
/ metabolism
Animals
CHO Cells
Chlorocebus aethiops
Cricetulus
Crystallography, X-Ray
Endoplasmic Reticulum
/ metabolism
Endoplasmic Reticulum Chaperone BiP
HEK293 Cells
Heat-Shock Proteins
/ chemistry
Humans
Models, Biological
Nerve Growth Factors
/ chemistry
Nucleotides
/ metabolism
Protein Binding
Protein Domains
Static Electricity
Unfolded Protein Response
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
01 02 2019
01 02 2019
Historique:
received:
22
08
2018
accepted:
11
01
2019
entrez:
3
2
2019
pubmed:
3
2
2019
medline:
2
4
2019
Statut:
epublish
Résumé
Despite its known role as a secreted neuroprotectant, much of the mesencephalic astrocyte-derived neurotrophic factor (MANF) is retained in the endoplasmic reticulum (ER) of producer cells. There, by unknown mechanisms, MANF plays a role in protein folding homeostasis in complex with the ER-localized Hsp70 chaperone BiP. Here we report that the SAF-A/B, Acinus, and PIAS (SAP) domain of MANF selectively associates with the nucleotide binding domain (NBD) of ADP-bound BiP. In crystal structures the SAP domain engages the cleft between NBD subdomains Ia and IIa, stabilizing the ADP-bound conformation and clashing with the interdomain linker that occupies this site in ATP-bound BiP. MANF inhibits both ADP release from BiP and ATP binding to BiP, and thereby client release. Cells lacking MANF have fewer ER stress-induced BiP-containing high molecular weight complexes. These findings suggest that MANF contributes to protein folding homeostasis as a nucleotide exchange inhibitor that stabilizes certain BiP-client complexes.
Identifiants
pubmed: 30710085
doi: 10.1038/s41467-019-08450-4
pii: 10.1038/s41467-019-08450-4
pmc: PMC6358605
doi:
Substances chimiques
Endoplasmic Reticulum Chaperone BiP
0
Heat-Shock Proteins
0
MANF protein, mouse
0
Nerve Growth Factors
0
Nucleotides
0
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
541Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
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