Amyloid-like aggregation of provasopressin in diabetes insipidus and secretory granule sorting.

ABSTRACT:

Background

Aggregation 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.

Results

Here 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

SUBMITTER: Beuret N 

PROVIDER: S-EPMC5267430 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature