ArticleJournal of molecular neuroscience : MN
Routing of membrane proteins to large dense core vesicles in PC12 cells.
Article in Journal of molecular neuroscience : MN. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Inside the Insulin Secretory Granule.Metabolites · 2021Review
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2 authors at 1 institution in 1 country.
Funding
Abstract
Routing of membrane proteins to large dense core vesicles in neuroendocrine cells can depend on information in both the lumenal and cytoplasmic domains. This study in PC12 cells focuses on the routing, cleavage, and secretion of an integral membrane protein, peptidylglycine alpha-amidating monooxygenase (PAM), examining both endogenous and virally derived membrane PAM. The role of the lumenal catalytic domains in membrane PAM trafficking was examined by replacement with an epitope tag. Virally derived membrane PAM is localized to the perinuclear area and to slender processes where the large dense core vesicles are located. Expression of PAM along with a neuroendocrine-specific endoprotease liberates a soluble monooxygenase domain, yielding regulated secretion of both the monooxygenase and the prohormone convertase from large dense core vesicles. The subcellular distribution of the epitope-substituted version of PAM within the cells is similar to that of membrane PAM, and both proteins are internalized from the plasma membrane. When secretion is stimulated, Serine937 in the cytoplasmic domain of PAM is phosphorylated to a similar extent in endogenous membrane PAM, virally encoded membrane PAM, and epitope-substituted PAM. Thus, the lumenal PAM catalytic domains are not required for routing or phosphorylation of PAM in PC12 cells.
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