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• W2912354675 abstract "Abstract 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." @default.
• W2912354675 created "2019-02-21" @default.
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• W2912354675 date "2019-02-01" @default.
• W2912354675 modified "2023-10-01" @default.
• W2912354675 title "MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP" @default.
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• W2912354675 doi "https://doi.org/10.1038/s41467-019-08450-4" @default.
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