ArticleBMC biology2017
Amyloid-like aggregation of provasopressin in diabetes insipidus and secretory granule sorting.
Article in BMC biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 27 citations in OpenAlex.
- Investigation of Fibrillar Aggregates Formed by Pathogenic Pre-pro-vasopressin Mutants that Cause ADNDI.The Journal of clinical endocrinology and metabolism · 2025Article
- Extraventricular Neurocytoma of the Sellar Region Presenting With Syndrome of Inappropriate Antidiuresis.JCEM case reports · 2024Article
- Small disulfide loops in peptide hormones mediate self-aggregation and secretory granule sorting.Life science alliance · 2022Article
- Article
- Protein Aggregation and Disaggregation in Cells and Development.Journal of molecular biology · 2021Review
- FERARI is required for Rab11-dependent endocytic recycling.Nature cell biology · 2020Article
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
- ICA512 RESP18 homology domain is a protein-condensing factor and insulin fibrillation inhibitor.The Journal of biological chemistry · 2019Article
- Maize 16-kD γ-zein forms very unusual disulfide-bonded polymers in the endoplasmic reticulum: implications for prolamin evolution.Journal of experimental botany · 2018Article
- A versatile nanobody-based toolkit to analyze retrograde transport from the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mice deficient for ERAD machinery component Sel1L develop central diabetes insipidus.The Journal of clinical investigation · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAggregation of peptide hormone precursors in the trans-Golgi network is an essential process in the biogenesis of secretory granules in endocrine cells. It has recently been proposed that this aggregation corresponds to the formation of functional amyloids. Our previous finding that dominant mutations in provasopressin, which cause cell degeneration and diabetes insipidus, prevent native folding and produce fibrillar aggregates in the endoplasmic reticulum (ER) might thus reflect mislocalized amyloid formation by sequences that evolved to mediate granule sorting.
resultsHere we identified two sequences responsible for fibrillar aggregation of mutant precursors in the ER: the N-terminal vasopressin nonapeptide and the C-terminal glycopeptide. To test their role in granule sorting, the glycopeptide was deleted and/or vasopressin mutated to inactivate ER aggregation while still permitting precursor folding and ER exit. These mutations strongly reduced sorting into granules and regulated secretion in endocrine AtT20 cells.
conclusionThe same sequences - vasopressin and the glycopeptide - mediate physiological aggregation of the wild-type hormone precursor into secretory granules and the pathological fibrillar aggregation of disease mutants in the ER. These findings support the amyloid hypothesis for secretory granule biogenesis.
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