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https://www.readbyqxmd.com/read/28515296/hepatitis-c-virus-lipoviroparticles-hcv-lvp-assemble-in-the-endoplasmic-reticulum-er-and-bud-off-from-the-er-to-golgi-in-copii-vesicles
#1
Gulam H Syed, Mohsin Khan, Song Yang, Aleem Siddiqui
Hepatitis C virus (HCV) exists as a lipoprotein-virus hybrid lipoviroparticle (LVP). In vitro studies have demonstrated the importance of apolipoproteins in HCV secretion and infectivity leading to the notion that HCV co-opts the secretion of very-low density lipoprotein (VLDL) for its egress. However, our understanding of the mechanisms involved in virus particle assembly and egress, are still elusive. Biogenesis of VLDL particle occurs in the ER followed by subsequent lipidation in the ER and Golgi. Secretion of mature VLDL particles occurs through the Golgi secretory pathway...
May 17, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28515233/wntless-sec12-complex-on-er-membrane-regulates-early-wnt-secretory-vesicle-assembly-and-mature-ligand-export
#2
Jiaxin Sun, Shiyan Yu, Xiao Zhang, Catherine Capac, Onyedikachi Aligbe, Timothy Daudelin, Edward M Bonder, Nan Gao
Wntless (Wls) transports Wnt molecules for secretion, however the cellular mechanism underlying the initial assembly of Wnt secretory vesicles is still not fully defined. Using proteomic and mutagenic analyses of the mammalian Wls, we report a mechanism for formation of early Wnt secretory vesicle on ER membrane. Wls forms a complex with SEC12, an ER membrane-localized GEF activator of SAR1 small GTPase. Compared to palmitoylation-deficient Wnt molecules, binding of mature Wnt to Wls increases Wls-SEC12 interaction and promotes Wls association with SAR1, the key activator of the COPII machinery...
May 17, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28500182/upr-transducer-bbf2h7-allows-export-of-type-ii-collagen-in-a-cargo-and-developmental-stage-specific-manner
#3
Tokiro Ishikawa, Takuya Toyama, Yuki Nakamura, Kentaro Tamada, Hitomi Shimizu, Satoshi Ninagawa, Tetsuya Okada, Yasuhiro Kamei, Tomoko Ishikawa-Fujiwara, Takeshi Todo, Eriko Aoyama, Masaharu Takigawa, Akihiro Harada, Kazutoshi Mori
The unfolded protein response (UPR) handles unfolded/misfolded proteins accumulated in the endoplasmic reticulum (ER). However, it is unclear how vertebrates correctly use the total of ten UPR transducers. We have found that ER stress occurs physiologically during early embryonic development in medaka fish and that the smooth alignment of notochord cells requires ATF6 as a UPR transducer, which induces ER chaperones for folding of type VIII (short-chain) collagen. After secretion of hedgehog for tissue patterning, notochord cells differentiate into sheath cells, which synthesize type II collagen...
May 12, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28499723/a-dual-site-gateway-cloning-system-for-simultaneous-cloning-of-two-genes-for-plant-transformation
#4
Mostafa Aboulela, Yuji Tanaka, Kohji Nishimura, Shoji Mano, Tetsuya Kimura, Tsuyoshi Nakagawa
Analyses of the subcellular localization of proteins and protein-protein interaction networks are essential to uncover the molecular basis of diverse biological processes in plants. To this end, we have created a Gateway cloning-compatible vector system, named dual-site (DS) Gateway cloning system to allow simple cloning of two expression cassettes in a binary vector and to express them simultaneously in plant cells. In the DS Gateway cloning system, (i) a moderate constitutive nopaline synthase promoter (Pnos), which is much suitable for localization analysis, is used to guide each expression cassette, (ii) four series of vectors with different plant resistance markers are established, (iii) N-terminal fusion with 6 fluorescent proteins and 7 epitope tags is available, (iv) both N- and C-terminal fusions with split enhanced yellow fluorescent protein (EYFP) are possible for efficient detection of protein-protein interactions using a bimolecular fluorescence complementation (BiFC) assay...
May 9, 2017: Plasmid
https://www.readbyqxmd.com/read/28486929/ulk1-phosphorylates-sec23a-and-mediates-autophagy-induced-inhibition-of-er-to-golgi-traffic
#5
Wenjia Gan, Caiyun Zhang, Ka Yu Siu, Ayano Satoh, Julian A Tanner, Sidney Yu
BACKGROUND: Autophagy is an inducible autodigestive process that allows cells to recycle proteins and other materials for survival during stress and nutrient deprived conditions. The kinase ULK1 is required to activate this process. ULK1 phosphorylates a number of target proteins and regulates many cellular processes including the early secretory pathway. Recently, ULK1 has been demonstrated to phosphorylate Sec16 and affects the transport of serotonin transporter at the ER exit sites (ERES), but whether ULK1 may affect the transport of other cargo proteins and general secretion has not been fully addressed...
May 10, 2017: BMC Cell Biology
https://www.readbyqxmd.com/read/28442536/tango1-recruits-sec16-to-coordinately-organize-er-exit-sites-for-efficient-secretion
#6
Miharu Maeda, Toshiaki Katada, Kota Saito
Mammalian endoplasmic reticulum (ER) exit sites export a variety of cargo molecules including oversized cargoes such as collagens. However, the mechanisms of their assembly and organization are not fully understood. TANGO1L is characterized as a collagen receptor, but the function of TANGO1S remains to be investigated. Here, we show that direct interaction between both isoforms of TANGO1 and Sec16 is not only important for their correct localization but also critical for the organization of ER exit sites. The depletion of TANGO1 disassembles COPII components as well as membrane-bound ER-resident complexes, resulting in fewer functional ER exit sites and delayed secretion...
April 25, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28428367/copii-coated-membranes-function-as-transport-carriers-of-intracellular-procollagen-i
#7
Amita Gorur, Lin Yuan, Samuel J Kenny, Satoshi Baba, Ke Xu, Randy Schekman
The coat protein complex II (COPII) is essential for the transport of large cargo, such as 300-nm procollagen I (PC1) molecules, from the endoplasmic reticulum (ER) to the Golgi. Previous work has shown that the CUL3-KLHL12 complex increases the size of COPII vesicles at ER exit sites to more than 300 nm in diameter and accelerates the secretion of PC1. However, the role of large COPII vesicles as PC1 transport carriers was not unambiguously demonstrated. In this study, using stochastic optical reconstruction microscopy, correlated light electron microscopy, and live-cell imaging, we demonstrate the existence of mobile COPII-coated vesicles that completely encapsulate the cargo PC1 and are physically separated from ER...
April 20, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28410007/key-roles-of-arf-small-g-proteins-and-biosynthetic-trafficking-for-animal-development
#8
Francisco F Rodrigues, Tony J C Harris
Although biosynthetic trafficking can function constitutively, it also functions specifically for certain developmental processes. These processes require either a large increase to biosynthesis or the biosynthesis and targeted trafficking of specific players. We review the conserved molecular mechanisms that direct biosynthetic trafficking, and discuss how their genetic disruption affects animal development. Specifically, we consider Arf small G proteins, such as Arf1 and Sar1, and their coat effectors, COPI and COPII, and how these proteins promote biosynthetic trafficking for cleavage of the Drosophila embryo, the growth of neuronal dendrites and synapses, extracellular matrix secretion for bone development, lumen development in epithelial tubes, notochord and neural tube development, and ciliogenesis...
April 14, 2017: Small GTPases
https://www.readbyqxmd.com/read/28301741/mechanisms-of-autophagy-initiation
#9
James H Hurley, Lindsey N Young
Autophagy is the process of cellular self-eating by a double-membrane organelle, the autophagosome. A range of signaling processes converge on two protein complexes to initiate autophagy: the ULK1 (unc51-like autophagy activating kinase 1) protein kinase complex and the PI3KC3- C1 (class III phosphatidylinositol 3-kinase complex I) lipid kinase complex. Some 90% of the mass of these large protein complexes consists of noncatalytic domains and subunits, and the ULK1 complex has essential noncatalytic activities...
March 15, 2017: Annual Review of Biochemistry
https://www.readbyqxmd.com/read/28292851/new-insights-into-protein-secretion-tango1-runs-rings-around-the-copii-coat
#10
Benjamin S Glick
In this issue, Liu et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201611088) and Raote et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201608080) use super-resolution microscopy to visualize large COPII-coated endoplasmic reticulum (ER) export carriers. Rings of TANGO1 surround COPII, implicating TANGO1 in organizing ER exit sites and in regulating COPII coat dynamics and geometry.
April 3, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28287860/autophagosome-formation-where-the-secretory-and-autophagy-pathways-meet
#11
Juan Wang, Saralin Davis, Ming Zhu, Elizabeth A Miller, Susan Ferro-Novick
The upregulation of autophagosome formation in response to nutrient deprivation requires significant intracellular membrane rearrangements that are poorly understood. Recent findings have implicated COPII-coated vesicles, well known as ER-Golgi cargo transport carriers, as key players in macroautophagy. The role of COPII vesicles in macroautophagy and how they interact with autophagy-related (Atg) proteins was unknown. In our recent report, we show that during nutrient deprivation, phosphorylation of the membrane-distal surface of the COPII coat subunit Sec24 facilitates the interaction of Sec24 with the Atg machinery (specifically, Atg9) to regulate the abundance of autophagosomes during starvation...
February 15, 2017: Autophagy
https://www.readbyqxmd.com/read/28280122/tango1-spatially-organizes-er-exit-sites-to-control-er-export
#12
Min Liu, Zhi Feng, Hongmei Ke, Ying Liu, Tianhui Sun, Jianli Dai, Wenhong Cui, José Carlos Pastor-Pareja
Exit of secretory cargo from the endoplasmic reticulum (ER) takes place at specialized domains called ER exit sites (ERESs). In mammals, loss of TANGO1 and other MIA/cTAGE (melanoma inhibitory activity/cutaneous T cell lymphoma-associated antigen) family proteins prevents ER exit of large cargoes such as collagen. Here, we show that Drosophila melanogaster Tango1, the only MIA/cTAGE family member in fruit flies, is a critical organizer of the ERES-Golgi interface. Tango1 rings hold COPII (coat protein II) carriers and Golgi in close proximity at their center...
April 3, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28280121/tango1-assembles-into-rings-around-copii-coats-at-er-exit-sites
#13
Ishier Raote, Maria Ortega Bellido, Marinella Pirozzi, Chong Zhang, David Melville, Seetharaman Parashuraman, Timo Zimmermann, Vivek Malhotra
TANGO1 (transport and Golgi organization 1) interacts with CTAGE5 and COPII components Sec23/Sec24 and recruits ERGIC-53 (endoplasmic reticulum [ER]-Golgi intermediate compartment 53)-containing membranes to generate a mega-transport carrier for export of collagens and apolipoproteins from the ER. We now show that TANGO1, at the ER, assembles in a ring that encircles COPII components. The C-terminal, proline-rich domains of TANGO1 molecules in the ring are initially tilted onto COPII coats but appear to be pushed apart as the carrier grows...
April 3, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28240221/mammalian-trappiii-complex-positively-modulates-the-recruitment-of-sec13-31-onto-copii-vesicles
#14
Shan Zhao, Chun Man Li, Xiao Min Luo, Gavin Ka Yu Siu, Wen Jia Gan, Lin Zhang, William K K Wu, Hsiao Chang Chan, Sidney Yu
The Transport protein particle (TRAPP) complex is a tethering factor for COPII vesicle. Of three forms of TRAPP (TRAPPI, II and III) complexes identified so far, TRAPPIII has been largely considered to play a role in autophagy. While depletion of TRAPPIII specific subunits caused defects in the early secretory pathway and TRAPPIII might interact with components of the COPII vesicle coat, its exact role remains to be determined. In this study, we studied the function of TRAPPIII in early secretory pathway using a TRAPPIII-specific subunit, TRAPPC12, as starting point...
February 27, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28197529/specific-copii-vesicles-transport-er-membranes-to-sites-of-autophagosome-formation
#15
Veit Goder
The endoplasmic reticulum (ER) is considered a prominent membrane source for the formation of autophagosomes. Recent results from our laboratory revealed a cellular mechanism for the contribution of the ER to autophagosomes in yeast: membranes, together with unconventional membrane fusion machinery, are delivered to sites of autophagosome formation by specific coat protein complex II (COPII) vesicles.
2017: Molecular & Cellular Oncology
https://www.readbyqxmd.com/read/28160489/sec16-in-conventional-and-unconventional-exocytosis-working-at-the-interface-of-membrane-traffic-and-secretory-autophagy
#16
REVIEW
Bor Luen Tang
Sec16 is classically perceived to be a scaffolding protein localized to the transitional endoplasmic reticulum (tER) or the ER exit sites (ERES), and has a conserved function in facilitating coat protein II (COPII) complex-mediated ER exit. Recent findings have, however, pointed toward a role for Sec16 in unconventional exocytosis of certain membrane proteins, such as the Cystic fibrosis transmembrane conductance regulator (CFTR) in mammalian cells, and possibly also α-integrin in certain contexts of Drosophila development...
February 4, 2017: Journal of Cellular Physiology
https://www.readbyqxmd.com/read/28067262/sec16a-is-critical-for-both-conventional-and-unconventional-secretion-of-cftr
#17
He Piao, Jiyoon Kim, Shin Hye Noh, Hee-Seok Kweon, Joo Young Kim, Min Goo Lee
CFTR is a transmembrane protein that reaches the cell surface via the conventional Golgi mediated secretion pathway. Interestingly, ER-to-Golgi blockade or ER stress induces alternative GRASP-mediated, Golgi-bypassing unconventional trafficking of wild-type CFTR and the disease-causing ΔF508-CFTR, which has folding and trafficking defects. Here, we show that Sec16A, the key regulator of conventional ER-to-Golgi transport, plays a critical role in the ER exit of protein cargos during unconventional secretion...
January 9, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28025315/%C3%AE-2-cop-is-involved-in-early-secretory-traffic-in-arabidopsis-and-is-required-for-plant-growth
#18
Fátima Gimeno-Ferrer, Noelia Pastor-Cantizano, César Bernat-Silvestre, Pilar Selvi-Martínez, Francisco Vera-Sirera, Caiji Gao, Miguel Angel Perez-Amador, Liwen Jiang, Fernando Aniento, María Jesús Marcote
COP (coat protein) I-coated vesicles mediate intra-Golgi transport and retrograde transport from the Golgi to the endoplasmic reticulum. These vesicles form through the action of the small GTPase ADP-ribosylation factor 1 (ARF1) and the COPI heptameric protein complex (coatomer), which consists of seven subunits (α-, β-, β'-, γ-, δ-, ε- and ζ-COP). In contrast to mammals and yeast, several isoforms for coatomer subunits, with the exception of γ and δ, have been identified in Arabidopsis. To understand the role of COPI proteins in plant biology, we have identified and characterized a loss-of-function mutant of α2-COP, an Arabidopsis α-COP isoform...
January 1, 2017: Journal of Experimental Botany
https://www.readbyqxmd.com/read/27872256/the-endosomal-transcriptional-regulator-rnf11-integrates-degradation-and-transport-of-egfr
#19
Sandra Scharaw, Murat Iskar, Alessandro Ori, Gaelle Boncompain, Vibor Laketa, Ina Poser, Emma Lundberg, Franck Perez, Martin Beck, Peer Bork, Rainer Pepperkok
Stimulation of cells with epidermal growth factor (EGF) induces internalization and partial degradation of the EGF receptor (EGFR) by the endo-lysosomal pathway. For continuous cell functioning, EGFR plasma membrane levels are maintained by transporting newly synthesized EGFRs to the cell surface. The regulation of this process is largely unknown. In this study, we find that EGF stimulation specifically increases the transport efficiency of newly synthesized EGFRs from the endoplasmic reticulum to the plasma membrane...
November 21, 2016: Journal of Cell Biology
https://www.readbyqxmd.com/read/27872251/regulation-of-egfr-surface-levels-by-copii-dependent-trafficking
#20
Hesso Farhan
Cell surface levels of epidermal growth factor receptors (EGFRs) are thought to be controlled mainly by endocytic trafficking, with biosynthetic EGFR trafficking presumed to be a constitutive and unregulated process. However, Scharaw et al. (2016. J. Cell Biol http://dx.doi.org/10.1083/jcb.201601090) demonstrate a role for inducible COPII trafficking in controlling EGFR surface levels.
November 21, 2016: Journal of Cell Biology
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