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https://www.readbyqxmd.com/read/28879181/regulation-of-the-sar1-gtpase-cycle-is-necessary-for-large-cargo-secretion-from-the-endoplasmic-reticulum
#1
REVIEW
Kota Saito, Miharu Maeda, Toshiaki Katada
Proteins synthesized within the endoplasmic reticulum (ER) are transported to the Golgi via coat protein complex II (COPII)-coated vesicles. The formation of COPII-coated vesicles is regulated by the GTPase cycle of Sar1. Activated Sar1 is recruited to ER membranes and forms a pre-budding complex with cargoes and the inner-coat complex. The outer-coat complex then stimulates Sar1 inactivation and completes vesicle formation. The mechanisms of forming transport carriers are well-conserved among species; however, in mammalian cells, several cargo molecules such as collagen, and chylomicrons are too large to be accommodated in conventional COPII-coated vesicles...
2017: Frontiers in Cell and Developmental Biology
https://www.readbyqxmd.com/read/28871045/loss-of-arabidopsis-p24-function-affects-erd2-traffic-and-golgi-structure-and-activates-the-unfolded-protein-response
#2
Noelia Pastor-Cantizano, Cesar Bernat-Silvestre, María Jesús Marcote, Fernando Aniento
p24 proteins are key regulators of protein trafficking along the secretory pathway but very little is known about their functions in plants. A quadruple loss-of-function mutant affecting the p24 genes from the δ-1 subclass of the p24 delta subfamily (p24δ3δ4δ5δ6) showed alterations in the Golgi apparatus, suggesting that these p24 proteins play a role in the organization of the compartments of the early secretory pathway in Arabidopsis Loss of p24δ-1 proteins also induced the accumulation of the K/HDEL receptor ERD2 at the Golgi apparatus and increased secretion of the ER chaperone BiP, an HDEL ligand, probably due to an inhibition of COPI-dependent Golgi-to-ER transport of ERD2 and thus retrieval of K/HDEL ligands...
September 4, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28869000/similarities-in-intracellular-transport-of-plant-viral-movement-proteins-bmb2-and-tgb3
#3
Ekaterina A Lazareva, Alexander A Lezzhov, Sergey A Golyshev, Sergey Y Morozov, Manfred Heinlein, Andrey G Solovyev
The cell-to-cell transport of many plant viruses through plasmodesmata requires viral movement proteins (MPs) encoded by a 'triple gene block' (TGB) and termed TGB1, TGB2 and TGB3. TGB3 is a small integral membrane protein that contains subcellular targeting signals and directs both TGB2 and the helicase domain-containing TGB1 protein to plasmodesmata-associated structures. Recently, we described a 'binary movement block' (BMB) coding for two MPs, BMB1 and BMB2. The BMB2 protein associates with endoplasmic reticulum (ER) membranes, accumulates at plasmodesmata-associated membrane bodies and directs the BMB1 helicase to these structures...
September 4, 2017: Journal of General Virology
https://www.readbyqxmd.com/read/28851831/tfg-facilitates-outer-coat-disassembly-on-copii-transport-carriers-to-promote-tethering-and-fusion-with-er-golgi-intermediate-compartments
#4
Michael G Hanna, Samuel Block, E B Frankel, Feng Hou, Adam Johnson, Lin Yuan, Gavin Knight, James J Moresco, John R Yates, Randolph Ashton, Randy Schekman, Yufeng Tong, Anjon Audhya
The conserved coat protein complex II (COPII) mediates the initial steps of secretory protein trafficking by assembling onto subdomains of the endoplasmic reticulum (ER) in two layers to generate cargo-laden transport carriers that ultimately fuse with an adjacent ER-Golgi intermediate compartment (ERGIC). Here, we demonstrate that Trk-fused gene (TFG) binds directly to the inner layer of the COPII coat. Specifically, the TFG C terminus interacts with Sec23 through a shared interface with the outer COPII coat and the cargo receptor Tango1/cTAGE5...
August 29, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28839076/golgi-entry-core-compartment-functions-as-the-copii-independent-scaffold-for-er-golgi-transport-in-plant-cells
#5
Yoko Ito, Tomohiro Uemura, Akihiko Nakano
Many questions remain about how the stacked structure of the Golgi apparatus is formed and maintained. In our previous study, we challenged this question using tobacco BY-2 cells and revealed that, upon Brefeldin A (BFA) treatment, previously undescribed small punctate structures containing a particular subset of cis-Golgi proteins are formed adjacent to the ER exit sites and act as the scaffold of Golgi regeneration after BFA removal. In this study, we have analyzed these structures further. The proteins that localize to these punctate structures originate from the cis-most cisternae...
August 24, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28801610/creb3l2-mediated-expression-of-sec23a-sec24d-is-involved-in-hepatic-stellate-cell-activation-through-er-golgi-transport
#6
Shotaro Tomoishi, Shinichi Fukushima, Kentaro Shinohara, Toshiaki Katada, Kota Saito
Hepatic fibrosis is caused by exaggerated wound healing response to chronic injury, which eventually leads to hepatic cirrhosis. Differentiation of hepatic stellate cells (HSCs) to myofibroblast-like cells by inflammatory cytokines is the critical step in fibrosis. This step is accompanied by enlargement of the endoplasmic reticulum (ER) and Golgi apparatus, suggesting that protein synthesis and secretion are augmented in the activated HSCs. However, the process of rearrangement of secretory organelles and their functions remain to be fully elucidated...
August 11, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28768830/neurodegeneration-associated-mutant-trem2-proteins-abortively-cycle-between-the-er-and-er-golgi-intermediate-compartment
#7
Daniel W Sirkis, Renan E Aparicio, Randy Schekman
Triggering receptor expressed on myeloid cells 2 (TREM2) is a transmembrane protein expressed on microglia within the brain. Several rare mutations in TREM2 cause an early-onset form of neurodegeneration when inherited homozygously. Here we investigate how these mutations affect the intracellular transport of TREM2. We find that most pathogenic TREM2 mutant proteins fail to undergo normal maturation in the Golgi complex and show markedly reduced cell surface expression. Prior research has suggested that two such mutants are retained in the endoplasmic reticulum (ER), but we find, using a cell-free COPII vesicle budding reaction, that mutant TREM2 is exported efficiently from the ER...
August 2, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28754694/remodeling-of-er-exit-sites-initiates-a-membrane-supply-pathway-for-autophagosome-biogenesis
#8
Liang Ge, Min Zhang, Samuel J Kenny, Dawei Liu, Miharu Maeda, Kota Saito, Anandita Mathur, Ke Xu, Randy Schekman
Autophagosomes are double-membrane vesicles generated during autophagy. Biogenesis of the autophagosome requires membrane acquisition from intracellular compartments, the mechanisms of which are unclear. We previously found that a relocation of COPII machinery to the ER-Golgi intermediate compartment (ERGIC) generates ERGIC-derived COPII vesicles which serve as a membrane precursor for the lipidation of LC3, a key membrane component of the autophagosome. Here we employed super-resolution microscopy to show that starvation induces the enlargement of ER-exit sites (ERES) positive for the COPII activator, SEC12, and the remodeled ERES patches along the ERGIC A SEC12 binding protein, CTAGE5, is required for the enlargement of ERES, SEC12 relocation to the ERGIC, and modulates autophagosome biogenesis...
September 2017: EMBO Reports
https://www.readbyqxmd.com/read/28747320/microscopic-analysis-of-reconstituted-copii-coat-polymerization-and-sec16-dynamics
#9
Hirohiko Iwasaki, Tomohiro Yorimitsu, Ken Sato
COPII coat and the small GTPase Sar1 mediate protein export from the endoplasmic reticulum (ER) via specialized domains known as the ER exit sites. The peripheral ER protein Sec16 has been proposed to organize ER exit sites. However, it remains unclear how these molecules drive COPII coat polymerization. Here, we characterized the spatiotemporal relationships between the COPII components during their polymerization using fluorescence microscopy combined with an artificial planar membrane. We demonstrated that Sar1 dissociates from the membrane shortly after the COPII coat recruitment, and Sar1 is then no longer required for the COPII coat to bind to the membrane...
July 26, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28727280/two-novel-effectors-of-trafficking-and-maturation-of-the-yeast-plasma-membrane-h-atpase
#10
Yosef Geva, Jonathan Crissman, Eric C Arakel, Natalia Gómez-Navarro, Silvia G Chuartzman, Kyle R Stahmer, Blanche Schwappach, Elizabeth A Miller, Maya Schuldiner
The endoplasmic reticulum (ER) is the entry site of proteins into the endomembrane system. Proteins exit the ER via coat protein II (COPII) vesicles in a selective manner, mediated either by direct interaction with the COPII coat or aided by cargo receptors. Despite the fundamental role of such receptors in protein sorting, only a few have been identified. To further define the machinery that packages secretory cargo and targets proteins from the ER to Golgi membranes, we used multiple systematic approaches, which revealed 2 uncharacterized proteins that mediate the trafficking and maturation of Pma1, the essential yeast plasma membrane proton ATPase...
July 20, 2017: Traffic
https://www.readbyqxmd.com/read/28723420/plant-and-yeast-cornichon-possess-a-conserved-acidic-motif-required-for-correct-targeting-of-plasma-membrane-cargos
#11
Paul Rosas-Santiago, Daniel Lagunas-Gomez, Carolina Yáñez-Domínguez, Rosario Vera-Estrella, Olga Zimmermannová, Hana Sychrová, Omar Pantoja
The export of membrane proteins along the secretory pathway is initiated at the endoplasmic reticulum after proteins are folded and packaged inside this organelle by their recruiting into the coat complex COPII vesicles. It is proposed that cargo receptors are required for the correct transport of proteins to its target membrane, however, little is known about ER export signals for cargo receptors. Erv14/Cornichon belong to a well conserved protein family in Eukaryotes, and have been proposed to function as cargo receptors for many transmembrane proteins...
July 16, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28713858/life-stage-specific-cargo-receptors-facilitate-glycosylphosphatidylinositol-anchored-surface-coat-protein-transport-in-trypanosoma-brucei
#12
Emilia K Kruzel, George P Zimmett, James D Bangs
The critical virulence factor of bloodstream-form Trypanosoma brucei is the glycosylphosphatidylinositol (GPI)-anchored variant surface glycoprotein (VSG). Endoplasmic reticulum (ER) exit of VSG is GPI dependent and relies on a discrete subset of COPII machinery (TbSec23.2/TbSec24.1). In other systems, p24 transmembrane adaptor proteins selectively recruit GPI-anchored cargo into nascent COPII vesicles. Trypanosomes have eight putative p24s (TbERP1 to TbERP8) that are constitutively expressed at the mRNA level...
July 2017: MSphere
https://www.readbyqxmd.com/read/28706295/dgk%C3%AE-triggers-endoplasmic-reticulum-release-of-ift88-containing-vesicles-destined-for-the-assembly-of-primary-cilia
#13
Jie Ding, Lei Shao, Yixing Yao, Xin Tong, Huaize Liu, Shen Yue, Lu Xie, Steven Y Cheng
The morphogenic factor Sonic hedgehog (Shh) signals through the primary cilium, which relies on intraflagellar transport to maintain its structural integrity and function. However, the process by which protein and lipid cargos are delivered to the primary cilium from their sites of synthesis still remains poorly characterized. Here, we report that diacylglycerol kinase δ (DGKδ), a residential lipid kinase in the endoplasmic reticulum, triggers the release of IFT88-containing vesicles from the ER exit sites (ERES), thereby setting forth their movement to the primary cilium...
July 13, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28700938/golgi-outpost-synthesis-impaired-by-toxic-polyglutamine-proteins-contributes-to-dendritic-pathology-in-neurons
#14
Chang Geon Chung, Min Jee Kwon, Keun Hye Jeon, Do Young Hyeon, Myeong Hoon Han, Jeong Hyang Park, In Jun Cha, Jae Ho Cho, Kunhyung Kim, Sangchul Rho, Gyu Ree Kim, Hyobin Jeong, Jae Won Lee, TaeSoo Kim, Keetae Kim, Kwang Pyo Kim, Michael D Ehlers, Daehee Hwang, Sung Bae Lee
Dendrite aberration is a common feature of neurodegenerative diseases caused by protein toxicity, but the underlying mechanisms remain largely elusive. Here, we show that nuclear polyglutamine (polyQ) toxicity resulted in defective terminal dendrite elongation accompanied by a loss of Golgi outposts (GOPs) and a decreased supply of plasma membrane (PM) in Drosophila class IV dendritic arborization (da) (C4 da) neurons. mRNA sequencing revealed that genes downregulated by polyQ proteins included many secretory pathway-related genes, including COPII genes regulating GOP synthesis...
July 11, 2017: Cell Reports
https://www.readbyqxmd.com/read/28697897/measuring-protein-binding-to-lipid-vesicles-by-fluorescence-cross-correlation-spectroscopy
#15
Daniela Krüger, Jan Ebenhan, Stefan Werner, Kirsten Bacia
Fluorescence correlation spectroscopy has been previously used to investigate peptide and protein binding to lipid membranes, as it allows for very low amounts of sample, short measurement times and equilibrium binding conditions. Labeling only one of the binding partners, however, comes with certain drawbacks, as it relies on identifying binding events by a change in diffusion coefficient. Since peptide and protein aggregation can obscure specific binding, and since non-stoichiometric binding necessitates the explicit choice of a statistical distribution for the number of bound ligands, we additionally label the liposomes and perform dual-color fluorescence cross-correlation spectroscopy (dcFCCS)...
July 8, 2017: Biophysical Journal
https://www.readbyqxmd.com/read/28696565/the-er-is-the-sorting-core-facility-in-the-golgi-lacking-protozoan-giardia-lamblia
#16
Nahuel Zamponi, Emiliano Zamponi, Gonzalo F Mayol, Adriana Lanfredi-Rangel, Staffan G Svärd, María C Touz
Our understanding of protein and lipid trafficking in eukaryotic cells has been challenged by the finding of different forms of compartmentalization and cargo processing in protozoan parasites. Here, we show that, in the absence of a Golgi compartment in Giardia, proteins destined for secretion are directly sorted and packaged at specialized ER regions enriched in COPII coatomer complexes and ceramide. We also demonstrated that ER-resident proteins are retained at the ER by the action of a KDEL receptor, which, in contrast to other eukaryotic KDEL receptors, showed no interorganellar dynamic but instead acts specifically at the limit of the ER membrane...
July 11, 2017: Traffic
https://www.readbyqxmd.com/read/28688928/transport-from-the-endoplasmic-reticulum-to-the-golgi-in-plants-where-are-we-now
#17
REVIEW
Federica Brandizzi
The biogenesis of about one third of the cellular proteome is initiated in the endoplasmic reticulum (ER), which exports proteins to the Golgi apparatus for sorting to their final destination. Notwithstanding the close proximity of the ER with other secretory membranes (e.g., endosomes, plasma membrane), the ER is also important for the homeostasis of non-secretory organelles such as mitochondria, peroxisomes, and chloroplasts. While how the plant ER interacts with most of the non-secretory membranes is largely unknown, the knowledge on the mechanisms for ER-to-Golgi transport is relatively more advanced...
July 5, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28679754/sec24c-dependent-transport-of-claudin-1-regulates-hepatitis-c-virus-entry
#18
Peiqi Yin, Ye Li, Leiliang Zhang
Claudin-1 is a hepatitis C virus (HCV) coreceptor required for viral entry. Although extensive studies have focused on claudin-1 as an anti-HCV target, little is known about how the level of claudin-1 at the cell surface is regulated by host vesicular transport. Here, we identified an interaction between claudin-1 and Sec24C, a cargo-sorting component of the coat protein complex II (COPII) vesicular transport system. By interacting with Sec24C through its C-terminal YV, claudin-1 is transported from the endoplasmic reticulum (ER) and is eventually targeted to the cell surface...
September 15, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28648601/inhibition-of-pld1-activity-causes-er-stress-via-regulation-of-copii-vesicle-formation
#19
Hiroshi Nakagawa, Kazuki Hazama, Katsumasa Ishida, Masayuki Komori, Kazuhiko Nishimura, Saburou Matsuo
Phospholipase D (PLD) plays a crucial role in the regulation of some cellular processes, including autophagy and apoptosis. Accumulation of protein in the endoplasmic reticulum (ER) lumen causes ER stress. Although ER stress is a principal cause of apoptosis and autophagy, the relationship between PLD activity and ER stress remains unclear. Protein transport from the ER to the Golgi apparatus is conducted by coat complex II (COPII) transport vesicles. Here, we demonstrated that inhibition of PLD1 activity or PLD1 knockdown suppressed COPII vesicle transport in normal rat kidney (NRK) cells...
August 26, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28626835/disrupted-er-to-golgi-trafficking-underlies-anti-hiv-drugs-and-alcohol-induced-cellular-stress-and-hepatic-injury
#20
Hui Han, Yuxin He, Jay Hu, Rhema Lau, Harrison Lee, Cheng Ji
Endoplasmic reticulum (ER) stress and unfolded protein response (UPR) are involved in anti-human immunodeficiency virus (HIV) drugs and alcohol-induced liver disease in a significant number of patients infected with HIV. However, the precise mechanism by which the drugs and alcohol cause ER stress remains elusive. We found that ritonavir-boosted lopinavir (RL) activated two canonical UPR branches without activation of the third canonical activating transcription factor 6 (ATF6) branch in either HepG2 cells or primary mouse hepatocytes...
April 2017: Hepatol Commun
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