Regulation of sumo mRNA during endoplasmic reticulum stress. by Kristin A Moore, Joshua J Plant, Deepika Gaddam, Jonathan Craft, Julie Hollien

“…The unfolded protein response (UPR) is a collection of pathways that maintains the protein secretory pathway during the many physiological and pathological conditions that cause stress in the endoplasmic reticulum (ER). …”
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A yeast model for amyloid-β aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity by Fabien D’Angelo, Hélène Vignaud, Julie Di Martino, Bénédicte Salin, Anne Devin, Christophe Cullin, Christelle Marchal

“…We sent this fusion protein into the secretory pathway and showed that intracellular traffic pathways are necessary for the generation of toxic species. …”
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The Plant V-ATPase by Thorsten Seidel

“…It contributes to cytosolic pH homeostasis and energizes transport processes across endomembranes of the secretory pathway. Its localization in the trans Golgi network/early endosomes is essential for vesicle transport, for instance for the delivery of cell wall components. …”
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Molecular characterization of malaria proteins involved in invasion of the host cell. by Liu, Bao Shan.

“…It might be transported to its respective location via the secretory pathway and is located neither in the microneme nor rhoptry site. …”
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The mammalian endoplasmic reticulum-associated degradation system. by Olzmann, J, Kopito, R, Christianson, J

“…The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic proteome and is accordingly endowed with specialized machinery to ensure that proteins deployed to the distal secretory pathway are correctly folded and assembled into native oligomeric complexes. …”

Rhomboid intramembrane protease RHBDL4 triggers ER-export and non-canonical secretion of membrane-anchored TGFα by Wunderle, L, Knopf, J, Kühnle, N, Morlé, A, Hehn, B, Adrain, C, Strisovsky, K, Freeman, M, Lemberg, M

“…We propose that RHBDL4 reorganizes trafficking events within the early secretory pathway in response to GPCR signaling. Our work identifies RHBDL4 as a rheostat that tunes secretion dynamics and abundance of specific membrane protein cargoes.…”

Structural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayer by Parker, J, Corey, R, Stansfeld, P, Newstead, S

“…Together these results provide further insight into how SLC35 family transporters function within the secretory pathway and sheds light onto the role that membrane lipids play in regulating transport across the membrane.…”

Perforin activity at membranes leads to invaginations and vesicle formation. by Praper, T, Sonnen, A, Kladnik, A, Andrighetti, A, Viero, G, Morris, K, Volpi, E, Lunelli, L, Dalla Serra, M, Froelich, C, Gilbert, R, Anderluh, G

“…The cytotoxic cell granule secretory pathway is essential for immune defence. How the pore-forming protein perforin (PFN) facilitates the cytosolic delivery of granule-associated proteases (granzymes) remains enigmatic. …”

Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity. by Brandhorst, D, Zwilling, D, Rizzoli, S, Lippert, U, Lang, T, Jahn, R

“…Membrane fusion in the secretory pathway is mediated by soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins. …”

A Two-Component Regulatory System Impacts Extracellular Membrane-Derived Vesicle Production in Group A Streptococcus by Ulrike Resch, James Anthony Tsatsaronis, Anaïs Le Rhun, Gerald Stübiger, Manfred Rohde, Sergo Kasvandik, Susanne Holzmeister, Philip Tinnefeld, Sun Nyunt Wai, Emmanuelle Charpentier

“…A comprehensive analysis of MV proteins identified both virulence-associated protein substrates of the general secretory pathway in addition to “anchorless surface proteins.” …”
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FRMD8 is a novel regulator of iRhom-dependent ADAM17 activity by Künzel, U

“…Interaction studies revealed that FRMD8 binds to the cytosolic N-terminus of iRhom2 throughout the entire secretory pathway. FRMD8 loss does not affect the ER-to-Golgi trafficking of iRhom2 but plays a role in stabilising iRhom2 at the plasma membrane by preventing the lysosomal degradation of both iRhom2 and mature ADAM17.…”

Secretion of a recombinant protein without a signal peptide by the exocrine glands of transgenic rabbits. by Andrea Kerekes, Orsolya Ivett Hoffmann, Gergely Iski, Nándor Lipták, Elen Gócza, Wilfried A Kues, Zsuzsanna Bősze, László Hiripi

“…The Sleeping Beauty (SB) transposon transgenic construct contains the Venus fluorophore cDNA, but without a signal peptide for the secretory pathway, driven by the ubiquitous CAGGS (CAG) promoter. …”
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The Physiological Functions of the Golgin Vesicle Tethering Proteins by Martin Lowe

“…Different golgins are localized to different regions of the Golgi, and their ability to selectively tether transport vesicles is important for the specificity of vesicle traffic in the secretory pathway. In recent years, our mechanistic understanding of golgin-mediated tethering has greatly improved. …”
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A genome-wide RNAi screen identifies regulators of cholesterol-modified hedgehog secretion in Drosophila. by Reid Aikin, Alexandra Cervantes, Gisela D'Angelo, Laurent Ruel, Sandra Lacas-Gervais, Sébastien Schaub, Pascal Thérond

“…We found that cholesterol-modified Hh secretion is strongly dependent on coat protein complex I (COPI) but not COPII vesicles, suggesting that cholesterol modification alters the movement of Hh through the early secretory pathway. We provide evidence that both proteolysis and cholesterol modification are necessary for the efficient trafficking of Hh through the ER and Golgi. …”
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Trafficking through COPII stabilises cell polarity and drives secretion during Drosophila epidermal differentiation. by Michaela Norum, Erika Tång, Tina Chavoshi, Heinz Schwarz, Dirk Linke, Anne Uv, Bernard Moussian

“…We show that they code for the Drosophila COPII vesicle-coating components Sec23 and Sec24, respectively, that organise vesicle transport from the ER to the Golgi apparatus.Taken together, epithelial differentiation during Drosophila embryogenesis is a concerted action of ECM formation, plasma membrane remodelling and maintenance of cell polarity that all three rely mainly, if not absolutely, on the canonical secretory pathway from the ER over the Golgi apparatus to the plasma membrane. …”
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PsVPS1, a dynamin-related protein, is involved in cyst germination and soybean infection of Phytophthora sojae. by Delong Li, Zhijian Zhao, Yidan Huang, Zhaojun Lu, Meng Yao, Yujuan Hao, Chunhua Zhai, Yuanchao Wang

“…This gene encodes a homolog of the Saccharomyces cerevisiae vacuolar protein sorting gene vps1 that mediates budding of clathrin-coated vesicles from the late Golgi, which are diverted from the general secretory pathway to the vacuole. PsVPS1-silenced mutants were generated using polyethylene glycol-mediated protoplast stable transformation and were viable but had reduced extracellular protein activity. …”
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Loss of Arabidopsis β-COP Function Affects Golgi Structure, Plant Growth and Tolerance to Salt Stress by Judit Sánchez-Simarro, César Bernat-Silvestre, Fátima Gimeno-Ferrer, Pilar Selvi-Martínez, Javier Montero-Pau, Fernando Aniento, María Jesús Marcote

“…The early secretory pathway involves bidirectional transport between the endoplasmic reticulum (ER) and the Golgi apparatus and is mediated by coat protein complex I (COPI)-coated and coat protein complex II (COPII)-coated vesicles. …”
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Transmissible Endoplasmic Reticulum Stress: A Novel Perspective on Tumor Immunity by Zhou Jiang, Geru Zhang, Liwei Huang, Yihang Yuan, Chenzhou Wu, Yi Li

“…As the first compartment of the protein secretory pathway, the endoplasmic reticulum (ER) acts as a protein synthesis factory, maintaining proteostasis and ER homeostasis. …”
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Golgi Metal Ion Homeostasis in Human Health and Diseases by Jie Li, Yanzhuang Wang

“…The homeostasis of metal ions in the secretory pathway, which is required for proper function and stress response of the Golgi, is tightly regulated and maintained by transporters. …”
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Intracellular peptides: From discovery to function by Emer S. Ferro, Vanessa Rioli, Leandro M. Castro, Lloyd D. Fricker

“…Peptidomics techniques have identified hundreds of peptides that are derived from proteins present mainly in the cytosol, mitochondria, and/or nucleus; these are termed intracellular peptides to distinguish them from secretory pathway peptides that function primarily outside of the cell. …”
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