Pro-hormone Secretogranin II Regulates Dense Core Secretory Granule Biogenesis in Catecholaminergic Cells

Courel, Maïté; Soler-Jover, Alejandro; Rodríguez-Flores, Juan L.; Mahata, Sushil K.; Élias, Salah; Montero-Hadjadje, Maïté; Anouar, Youssef; Giuly, Richard J.; O’Connor, Daniel T.; Taupenot, Laurent

doi:10.1074/jbc.m109.064196

Cited by 44 publications

(32 citation statements)

References 85 publications

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“…The granin proteins aggregate at low pH and high calcium concentrations (Chanat and Huttner 1991) and are capable of interacting with TGN-membrane components and drive the sorting of other proteins destined for DCVs (Mahapatra et al 2008;MonteroHadjadje et al 2009). It has been proposed that these protein aggregates, physically induce the TGN-membrane budding to form dense-core granules (MonteroHadjadje et al 2009;Courel et al 2010). In this process, HID-1 at the TGN might participate in the appropriate sorting of peptides into DCVs and/or in the induction of the DCVs budding.…”

Section: Discussionmentioning

confidence: 99%

HID-1, a New Component of the Peptidergic Signaling Pathway

et al. 2011

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hid-1 was originally identified as a Caenorhabditis elegans gene encoding a novel conserved protein that regulates the decision to enter into the enduring dauer larval stage. We isolated a novel allele of hid-1 in a forward genetic screen for mutants mislocalizing RBF-1 rabphilin, a RAB-27 effector. Here we demonstrate that HID-1 functions in the nervous system to regulate neuromuscular signaling and in the intestine to regulate the defecation motor program. We further show that a conserved N-terminal myristoylated motif of both invertebrate and vertebrate HID-1 is essential for its association with intracellular membranes in nematodes and PC12 cells. C. elegans neuronal HID-1 resides on intracellular membranes in neuronal cell somas; however, the kinesin UNC-104 also transports HID-1 to synaptic regions. HID-1 accumulates in the axons of unc-13 and unc-31 mutants, suggesting it is associated with neurosecretory vesicles. Consistent with this, genetic studies place HID-1 in a peptidergic signaling pathway. Finally, a hid-1 null mutation reduces the levels of endogenous neuropeptides and alters the secretion of fluorescent-tagged cargos derived from neuronal and intestinal dense core vesicles (DCVs). Taken together, our findings indicate that HID-1 is a novel component of a DCV-based neurosecretory pathway and that it regulates one or more aspects of the biogenesis, maturation, or trafficking of DCVs.

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Section: Discussionmentioning

confidence: 99%

HID-1, a New Component of the Peptidergic Signaling Pathway

et al. 2011

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“…Indeed, the knockdown of SgIII in pituitary-derived AtT-20 cells has disclosed a latent redundancy in the sorting and biosynthesis of SGs, where another granin protein, SgII, behaves like SgIII (Sun et al 2013). Conversely, after the knockdown of SgII in PC12 cells, the number of SGs significantly decreases but they are not completely depleted (Courel et al 2010). Furthermore, we have demonstrated that the interaction between SgIII and CPE facilitates prohormone sorting within SGs in CPE-deficient Cpe fat/fat mice, whose expression levels of SgIII and CgA are substantially elevated (Hosaka et al 2005).…”

Section: Discussionmentioning

confidence: 99%

Expression of Secretogranin III in Chicken Endocrine Cells

Gomi

Morikawa

Shinmura

et al. 2015

J Histochem Cytochem.

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The expression of secretogranin III (SgIII) in chicken endocrine cells has not been investigated. There is limited data available for the immunohistochemical localization of SgIII in the brain, pituitary, and pancreatic islets of humans and rodents. In the present study, we used immunoblotting to reveal the similarities between the expression patterns of SgIII in the common endocrine glands of chickens and rats. The protein–protein interactions between SgIII and chromogranin A (CgA) mediate the sorting of CgA/prohormone core aggregates to the secretory granule membrane. We examined these interactions using co-immunoprecipitation in chicken endocrine tissues. Using immunohistochemistry, we also examined the expression of SgIII in a wide range of chicken endocrine glands and gastrointestinal endocrine cells (GECs). SgIII was expressed in the pituitary, pineal, adrenal (medullary parts), parathyroid, and ultimobranchial glands, but not in the thyroid gland. It was also expressed in GECs of the stomach (proventriculus and gizzard), small and large intestines, and pancreatic islet cells. These SgIII-expressing cells co-expressed serotonin, somatostatin, gastric inhibitory polypeptide, glucagon-like peptide-1, glucagon, or insulin. These results suggest that SgIII is expressed in the endocrine cells that secrete peptide hormones, which mature via the intragranular enzymatic processing of prohormones and physiologically active amines in chickens.

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“…Granin expression correlates with granule biogenesis, indicating that a primary role of granins is to sort and pack DCGs. [9][10][11] However, granins are also prohormones that can be intra-and extragranularly proteolytically proces sed into various bioactive peptides. 12 The derived granin fragments are detectable in cerebrospinal fluid (CSF), thus making them attractive as potential biological markers of the neuronal regulatory secretory pathway.…”

Section: Introductionmentioning

confidence: 99%