Multiple Sorting Systems for Secretory Granules Ensure the Regulated Secretion of Peptide Hormones

Sun, Meng; Watanabe, Tsuyoshi; Bochimoto, Hiroki; Sakai, Yuko; Torii, Seiji; Takeuchi, Toshiyuki; Hosaka, Masahiro

doi:10.1111/tra.12029

Cited by 16 publications

(15 citation statements)

References 53 publications

(116 reference statements)

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“…However, we could not demonstrate binding of purified proglucagon to liposomes (data not shown) and therefore hypothesize that proglucagon may bind to granule proteins. It is possible that granins bind prohormones, such as pro-opiomelanocortin (64). We have some evidence that proglucagon sorting involves interaction with CPE in ␣ cells (33).…”

Section: Discussionmentioning

confidence: 84%

Two Dipolar α-Helices within Hormone-encoding Regions of Proglucagon Are Sorting Signals to the Regulated Secretory Pathway

Guizzetti¹,

McGirr

Dhanvantari

2014

Journal of Biological Chemistry

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Background:The constituent peptides of proglucagon contain ␣-helices that may target proglucagon to secretory granules. Results: Sorting of proglucagon processing intermediates is context-dependent, despite containing two sorted domains of glucagon and glucagon-like peptide 1. Conclusion: Proglucagon sorting is directed by two dipolar ␣-helices within glucagon and GLP-1. Significance: Hormone domains, rather than disordered prodomains, encode proglucagon sorting signals.

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Section: Discussionmentioning

confidence: 84%

Two Dipolar α-Helices within Hormone-encoding Regions of Proglucagon Are Sorting Signals to the Regulated Secretory Pathway

Guizzetti¹,

McGirr

Dhanvantari

2014

Journal of Biological Chemistry

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“…to provide the peptide hormone ready for secretion upon stimulation of the mature secretory granule. Hence, sorting of POMC to the granules of the RSP likely requires interaction with multiple membrane associated molecules, of which CPE and SgIII are primary candidates, in addition to SgII (Sun, et al 2013), at the lumenal side of the TGN during the initial budding and this interaction results in the active sorting and retention of the prohormone as the immature granule forms and matures.…”

Section: Intracellular Organization Of Pomc Maturationmentioning

confidence: 99%

60 YEARS OF POMC: Biosynthesis, trafficking, and secretion of pro-opiomelanocortin-derived peptides

Cawley

Loh

2016

Journal of Molecular Endocrinology

142

127

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Pro-opiomelanocortin (POMC) is a prohormone that encodes multiple smaller peptide hormones within its structure. These peptide hormones can be generated by cleavage of POMC at basic-residue cleavage sites by prohormone converting enzymes in the regulated secretory pathway of POMC synthesizing endocrine cells and neurons. The peptides are stored inside the cells in dense core secretory granules until released in a stimulus dependent manner. The complexity of the regulation of the biosynthesis, trafficking and secretion of POMC and its peptides reflect an impressive level of control over many factors involved in the ultimate role of POMC expressing cells, i.e. to produce a range of different biologically active peptide hormones ready for action when signaled by the body. From the discovery of POMC as the precursor to ACTH and β-Lipotropin in the late 1970s to our current knowledge, the understanding of POMC physiology remains a monumental body of work that has provided insight into many aspects of molecular endocrinology. In this chapter, we describe the intracellular trafficking of POMC in endocrine cells, its sorting into dense core secretory granules and transport of these granules to the regulated secretory pathway. Additionally, we review the enzymes involved in the maturation of POMC to its various peptides and the mechanisms involved in the differential processing of POMC in different cell types. Finally, we highlight studies pertaining to the regulation of ACTH secretion in the anterior and intermediate pituitary and POMC neurons of the hypothalamus.

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“…; Sun et al . ). Cgs are the most abundant constituents of DCVs intravesicular matrix (Taupenot et al .…”

mentioning

confidence: 97%

Dense‐core vesicle biogenesis and exocytosis in neurons lacking chromogranins A and B

Domínguez

Weering

Borges

et al. 2017

Journal of Neurochemistry

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Multiple Sorting Systems for Secretory Granules Ensure the Regulated Secretion of Peptide Hormones

Cited by 16 publications

References 53 publications

Two Dipolar α-Helices within Hormone-encoding Regions of Proglucagon Are Sorting Signals to the Regulated Secretory Pathway

Two Dipolar α-Helices within Hormone-encoding Regions of Proglucagon Are Sorting Signals to the Regulated Secretory Pathway

60 YEARS OF POMC: Biosynthesis, trafficking, and secretion of pro-opiomelanocortin-derived peptides

Dense‐core vesicle biogenesis and exocytosis in neurons lacking chromogranins A and B

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