Dense-Core Secretory Granule Biogenesis

Physiology ◽  
2006 ◽  
Vol 21 (2) ◽  
pp. 124-133 ◽  
Author(s):  
Taeyoon Kim ◽  
Marjorie C. Gondré-Lewis ◽  
Irina Arnaoutova ◽  
Y. Peng Loh
Keyword(s):  
Secretory Granule ◽  
Endocrine Cells ◽  
Dense Core ◽  
Trans Golgi Network ◽  
Golgi Network

The dense-core secretory granule is a key organelle for secretion of hormones and neuropeptides in endocrine cells and neurons, in response to stimulation. Cholesterol and granins are critical for the assembly of these organelles at the trans-Golgi network, and their biogenesis is regulated quantitatively by posttranscriptional and posttranslational mechanisms.

scholarly journals HID-1 controls formation of large dense core vesicles by influencing cargo sorting and trans-Golgi network acidification

2017 ◽  
Vol 28 (26) ◽  
pp. 3870-3880 ◽  
Author(s):  
Blake H. Hummer ◽  
Noah F. de Leeuw ◽  
Christian Burns ◽  
Lan Chen ◽  
Matthew S. Joens ◽  
...  
Keyword(s):  
Biochemical Properties ◽  
Neuroendocrine Cells ◽  
Dense Core ◽  
Core Formation ◽  
Dense Core Vesicles ◽  
Atpase Subunit ◽  
Trans Golgi Network ◽  
Large Dense Core Vesicles ◽  
Golgi Network ◽  
Cargo Sorting

Large dense core vesicles (LDCVs) mediate the regulated release of neuropeptides and peptide hormones. They form at the trans-Golgi network (TGN), where their soluble content aggregates to form a dense core, but the mechanisms controlling biogenesis are still not completely understood. Recent studies have implicated the peripheral membrane protein HID-1 in neuropeptide sorting and insulin secretion. Using CRISPR/Cas9, we generated HID-1 KO rat neuroendocrine cells, and we show that the absence of HID-1 results in specific defects in peptide hormone and monoamine storage and regulated secretion. Loss of HID-1 causes a reduction in the number of LDCVs and affects their morphology and biochemical properties, due to impaired cargo sorting and dense core formation. HID-1 KO cells also exhibit defects in TGN acidification together with mislocalization of the Golgi-enriched vacuolar H+-ATPase subunit isoform a2. We propose that HID-1 influences early steps in LDCV formation by controlling dense core formation at the TGN.

scholarly journals Differential sorting behavior for soluble and transmembrane cargoes at the trans-Golgi network in endocrine cells

2020 ◽  
Vol 31 (3) ◽  
pp. 157-166 ◽  
Author(s):  
Blake H. Hummer ◽  
Drew Maslar ◽  
Margarita Soltero-Gutierrez ◽  
Noah F. de Leeuw ◽  
Cedric S. Asensio
Keyword(s):  
Endocrine Cells ◽  
Secretory Granules ◽  
Complex Model ◽  
Trans Golgi Network ◽  
Golgi Network

Formation of secretory granules (SGs) occurs at the trans-Golgi network (TGN). Here we show that transmembrane SG cargoes (phogrin and VMAT2) do not sort directly onto SGs during budding, but rather exit the TGN into nonregulated vesicles to get incorporated to SGs at a later step, suggesting a more complex model of SG biogenesis than anticipated.

scholarly journals Differential sorting behavior for soluble and transmembrane cargoes at the trans-Golgi network in endocrine cells

2019 ◽  
Author(s):  
Blake H. Hummer ◽  
Drew Maslar ◽  
Margarita Soltero Gutierrez ◽  
Noah F. de Leeuw ◽  
Cedric S. Asensio
Keyword(s):  
Endocrine Cells ◽  
Secretory Granules ◽  
Complex Model ◽  
Secreted Proteins ◽  
Secretory Pathways ◽  
Regulated Secretion ◽  
Trans Golgi Network ◽  
Differential Behavior ◽  
Golgi Network ◽  
Kinetics Of

AbstractRegulated secretion of neuropeptides and peptide hormones by secretory granules (SGs) is central to physiology. Formation of SGs occurs at the trans-Golgi network (TGN) where their soluble cargo aggregates to form a dense core, but the mechanisms controlling the sorting of regulated secretory cargoes (soluble and transmembrane) away from constitutively secreted proteins remain unclear. Optimizing the use of the retention using selective hooks (RUSH) method in (neuro-)endocrine cells, we now quantify TGN budding kinetics of constitutive and regulated secretory cargoes. We further show that, by monitoring two cargoes simultaneously, it becomes possible to visualize sorting to the constitutive and regulated secretory pathways in real-time. Further analysis of the localization of SG cargoes immediately after budding from the TGN revealed that, surprisingly, the bulk of two studied transmembrane SG cargoes (phogrin and VMAT2) does not sort directly onto SGs during budding, but rather exit the TGN into non-regulated vesicles to get incorporated to SGs at a later step. This differential behavior of soluble and transmembrane cargoes suggests a more complex model of SG biogenesis than anticipated.

scholarly journals The BAR Domain Protein Arfaptin-1 Controls Secretory Granule Biogenesis at the trans-Golgi Network

2012 ◽  
Vol 23 (4) ◽  
pp. 756-768 ◽  
Author(s):  
Helmuth Gehart ◽  
Alexander Goginashvili ◽  
Rainer Beck ◽  
Joëlle Morvan ◽  
Eric Erbs ◽  
...  
Keyword(s):  
Secretory Granule ◽  
Bar Domain ◽  
Trans Golgi Network ◽  
Domain Protein ◽  
Golgi Network

scholarly journals Formation of secretory vesicles in permeabilized cells: a salt extract from yeast membranes promotes budding of nascent secretory vesicles from the trans-Golgi network of endocrine cells

1996 ◽  
Vol 314 (3) ◽  
pp. 723-726 ◽  
Author(s):  
Wai Lam W. LING ◽  
Dennis SHIELDS
Keyword(s):  
Mammalian Cells ◽  
Endocrine Cells ◽  
Secretory Vesicle ◽  
Gh3 Cells ◽  
Vesicle Formation ◽  
Secretory Vesicles ◽  
Vesicle Budding ◽  
Trans Golgi Network ◽  
Golgi Network ◽  
Salt Extract

The mechanism of secretory-vesicle formation from the trans-Golgi network (TGN) of endocrine cells is poorly understood. To identify cytosolic activities that facilitate the formation and fission of nascent secretory vesicles, we treated permeabilized pituitary GH3 cells with high salt to remove endogenous budding factors. Using this cell preparation, secretory-vesicle budding from the TGN required addition of exogenous cytosol and energy. Mammalian cytosols (GH3 cells and bovine brain) promoted post-TGN vesicle formation. Most significantly, a salt extract of membranes from the yeast Saccharomyces cerevisiae, a cell lacking a regulated secretory pathway, stimulated secretory vesicle budding in the absence of mammalian cytosolic factors. These results demonstrate that the factors which promote secretory-vesicle release from the TGN are conserved between yeast and mammalian cells.

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