ArticleMolecular and cellular endocrinology2007
The transmembrane domain of the prohormone convertase PC3: a key motif for targeting to the regulated secretory pathway.
Article in Molecular and cellular endocrinology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications.Science signaling · 2021Review
- A human carboxypeptidase E/NF-α1 gene mutation in an Alzheimer's disease patient leads to dementia and depression in mice.Translational psychiatry · 2016Article
- γ-Adducin promotes process outgrowth and secretory protein exit from the Golgi apparatus.Journal of molecular neuroscience : MN · 2013Article
- Cholesterol-enriched membrane rafts and insulin secretion.Journal of diabetes investigation · 2012Review
- Exploring the membrane topology of prohormone convertase 1 in AtT20 Cells: in situ analysis by immunofluorescence microscopy.F1000Research · 2012Article
- Carboxypeptidase E cytoplasmic tail mediates localization of synaptic vesicles to the pre-active zone in hypothalamic pre-synaptic terminals.Journal of neurochemistry · 2010Article
- Functional and structural characterization of a dense core secretory granule sorting domain from the PC1/3 protease.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Pax6 regulates the proglucagon processing enzyme PC2 and its chaperone 7B2.Molecular and cellular biology · 2009Article
- Sorting of growth hormone-erythropoietin fusion proteins in rat salivary glands.Biochemical and biophysical research communications · 2008Article
- Sorting behavior of a transgenic erythropoietin-growth hormone fusion protein in murine salivary glands.Human gene therapy · 2008Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The biosynthesis of hormones and neuropeptides involves post-translational cleavage of precursors at basic amino acids by prohormone convertases (PCs) predominantly in secretory granules that bud from the trans-Golgi Network. This study reports that the amino acid sequence of PC3 (aa617-638), previously identified as a novel transmembrane (TM) domain, confers lipid raft association and facilitates sorting of the enzyme to the secretory granules of Neuro2A cells for prohormone cleavage. Floatation analysis on sucrose density gradients showed that a proportion of full length (PC3-FL) and carboxyl terminus-truncated PC3(1-638) (PC3-638) containing the TM domain were associated with lipid rafts in Neuro2A cells, while PC3(1-616) (PC3-616) and PC3-DeltaTM lacking the TM domain were not. Secondly, PC3-FL and PC3-638 underwent stimulated secretion and were shown to be colocalized with a secretory granule marker, chromogranin A, by immunocytochemistry. In contrast, PC3-616 and PC3-DeltaTM were constitutively secreted and primarily localized in the Golgi. These data indicate that the transmembrane domain of PC3 plays a key role in sorting the enzyme to the regulated secretory pathway.
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