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Journal articles on the topic 'VAP proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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1

Jacks, Stephanie, Steeve Giguère, and John F. Prescott. "In Vivo Expression of and Cell-Mediated Immune Responses to the Plasmid-Encoded Virulence-Associated Proteins of Rhodococcus equi in Foals." Clinical and Vaccine Immunology 14, no. 4 (2007): 369–74. http://dx.doi.org/10.1128/cvi.00448-06.

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ABSTRACT Rhodococcus equi is a facultative intracellular pathogen that causes pneumonia in foals but does not induce disease in adult horses. Virulence of R. equi depends on the presence of a large plasmid, which encodes a family of seven virulence-associated proteins (VapA and VapC to VapH). Eradication of R. equi from the lungs depends on gamma interferon (IFN-γ) production by T lymphocytes. The objectives of the present study were to determine the relative in vivo expression of the vap genes of R. equi in the lungs of infected foals, to determine the recall response of bronchial lymph node

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2

Byrne, Barbara A., John F. Prescott, Guy H. Palmer, et al. "Virulence Plasmid of Rhodococcus equiContains Inducible Gene Family Encoding Secreted Proteins." Infection and Immunity 69, no. 2 (2001): 650–56. http://dx.doi.org/10.1128/iai.69.2.650-656.2001.

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ABSTRACT Rhodococcus equi causes severe pyogranulomatous pneumonia in foals. This facultative intracellular pathogen produces similar lesions in immunocompromised humans, particularly in AIDS patients. Virulent strains of R. equi bear a large plasmid that is required for intracellular survival within macrophages and for virulence in foals and mice. Only two plasmid-encoded proteins have been described previously; a 15- to 17-kDa surface protein designated virulence-associated protein A (VapA) and an antigenically related 20-kDa protein (herein designated VapB). These two proteins are not expre

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3

Hooper-McGrevy, Kathleen E., Bruce N. Wilkie, and John F. Prescott. "Immunoglobulin G Subisotype Responses of Pneumonic and Healthy, Exposed Foals and Adult Horses to Rhodococcus equi Virulence-Associated Proteins." Clinical Diagnostic Laboratory Immunology 10, no. 3 (2003): 345–51. http://dx.doi.org/10.1128/cdli.10.3.345-351.2003.

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ABSTRACT Rhodococcus equi causes severe pyogranulomatous pneumonia in foals and in immunocompromised humans. Replication of virulent isolates within macrophages correlates with the presence of a large plasmid which encodes a family of seven virulence-associated proteins (VapA and VapC to VapH), whose functions are unknown. Although cell-mediated immunity is thought to be crucial in eliminating R. equi infection, antibody partially protects foals. The antibody response to both VapA and VapC was similar in six adult horses and six naturally exposed but healthy foals, as well as in eight foals wi

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4

Hua, Rong, Derrick Cheng, Étienne Coyaud, et al. "VAPs and ACBD5 tether peroxisomes to the ER for peroxisome maintenance and lipid homeostasis." Journal of Cell Biology 216, no. 2 (2017): 367–77. http://dx.doi.org/10.1083/jcb.201608128.

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Lipid exchange between the endoplasmic reticulum (ER) and peroxisomes is necessary for the synthesis and catabolism of lipids, the trafficking of cholesterol, and peroxisome biogenesis in mammalian cells. However, how lipids are exchanged between these two organelles is not understood. In this study, we report that the ER-resident VAMP-associated proteins A and B (VAPA and VAPB) interact with the peroxisomal membrane protein acyl-CoA binding domain containing 5 (ACBD5) and that this interaction is required to tether the two organelles together, thereby facilitating the lipid exchange between t

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5

Geerds, Christina, Jens Wohlmann, Albert Haas та Hartmut H. Niemann. "Structure ofRhodococcus equivirulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs". Acta Crystallographica Section F Structural Biology Communications 70, № 7 (2014): 866–71. http://dx.doi.org/10.1107/s2053230x14009911.

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Members of the virulence-associated protein (Vap) family from the pathogenRhodococcus equiregulate virulence in an unknown manner. They do not share recognizable sequence homology with any protein of known structure. VapB and VapA are normally associated with isolates from pigs and horses, respectively. To contribute to a molecular understanding of Vap function, the crystal structure of a protease-resistant VapB fragment was determined at 1.4 Å resolution. The structure was solved by SAD phasing employing the anomalous signal of one endogenous S atom and two bound Co ions with low occupancy. V

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Letek, Michal, Alain A. Ocampo-Sosa, Mandy Sanders, et al. "Evolution of the Rhodococcus equi vap Pathogenicity Island Seen through Comparison of Host-Associated vapA and vapB Virulence Plasmids." Journal of Bacteriology 190, no. 17 (2008): 5797–805. http://dx.doi.org/10.1128/jb.00468-08.

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ABSTRACT The pathogenic actinomycete Rhodococcus equi harbors different types of virulence plasmids associated with specific nonhuman hosts. We determined the complete DNA sequence of a vapB + plasmid, typically associated with pig isolates, and compared it with that of the horse-specific vapA + plasmid type. pVAPB1593, a circular 79,251-bp element, had the same housekeeping backbone as the vapA + plasmid but differed over an ≈22-kb region. This variable region encompassed the vap pathogenicity island (PAI), was clearly subject to selective pressures different from those affecting the backbone

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Voilquin, Laetitia, Massimo Lodi, Thomas Di Mattia, et al. "STARD3: A Swiss Army Knife for Intracellular Cholesterol Transport." Contact 2 (January 2019): 251525641985673. http://dx.doi.org/10.1177/2515256419856730.

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Intracellular cholesterol transport is a complex process involving specific carrier proteins. Cholesterol-binding proteins, such as the lipid transfer protein steroidogenic acute regulatory-related lipid transfer domain-3 (STARD3), are implicated in cholesterol movements between organelles. Indeed, STARD3 modulates intracellular cholesterol allocation by reducing it from the plasma membrane and favoring its passage from the endoplasmic reticulum (ER) to endosomes, where the protein is localized. STARD3 interacts with ER-anchored partners, notably vesicle-associated membrane protein-associated

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8

Johnson, Ben, Ashley N. Leek, Laura Solé, Emily E. Maverick, Tim P. Levine, and Michael M. Tamkun. "Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB." Proceedings of the National Academy of Sciences 115, no. 31 (2018): E7331—E7340. http://dx.doi.org/10.1073/pnas.1805757115.

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Kv2.1 exhibits two distinct forms of localization patterns on the neuronal plasma membrane: One population is freely diffusive and regulates electrical activity via voltage-dependent K+ conductance while a second one localizes to micrometer-sized clusters that contain densely packed, but nonconducting, channels. We have previously established that these clusters represent endoplasmic reticulum/plasma membrane (ER/PM) junctions that function as membrane trafficking hubs and that Kv2.1 plays a structural role in forming these membrane contact sites in both primary neuronal cultures and transfect

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9

Wilhelm, Léa P., Catherine Tomasetto, and Fabien Alpy. "Touché! STARD3 and STARD3NL tether the ER to endosomes." Biochemical Society Transactions 44, no. 2 (2016): 493–98. http://dx.doi.org/10.1042/bst20150269.

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Membrane contact sites (MCSs) are subcellular regions where the membranes of distinct organelles come into close apposition. These specialized areas of the cell, which are involved in inter-organelle metabolite exchange, are scaffolded by specific complexes. STARD3 [StAR (steroidogenic acute regulatory protein)-related lipid transfer domain-3] and its close paralogue STARD3NL (STARD3 N-terminal like) are involved in the formation of contacts between late-endosomes and the endoplasmic reticulum (ER). The lipid transfer protein (LTP) STARD3 and STARD3NL, which are both anchored on the limiting m

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10

Barton, N. R., E. M. Bonder, D. J. Fishkind, R. H. Warren, and M. M. Pratt. "A novel vesicle-associated protein (VAP-1) in sea urchin eggs containing multiple RNA-binding consensus sequences." Journal of Cell Science 103, no. 3 (1992): 797–809. http://dx.doi.org/10.1242/jcs.103.3.797.

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We have identified a novel high molecular weight, vesicle-associated protein (VAP-1) in the eggs of the sea urchin Strongylocentrotus purpuratus. Biochemical fractionation and immunofluorescence analysis of unfertilized eggs indicate that VAP-1 is a peripheral membrane protein associated with microsomal membrane fractions. Sequence analysis of partial VAP-1 cDNA clones reveals that the protein contains at least four RNA-binding consensus sequences. The RNA-binding sequences are separated by several glycine rich domains and this organization, RNA-binding domains separated by glycine rich sequen

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11

James, Christina, and Ralph H. Kehlenbach. "The Interactome of the VAP Family of Proteins: An Overview." Cells 10, no. 7 (2021): 1780. http://dx.doi.org/10.3390/cells10071780.

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Membrane contact sites (MCS) are sites of close apposition of two organelles that help in lipid transport and synthesis, calcium homeostasis and several other biological processes. The VAMP-associated proteins (VAPs) VAPA, VAPB, MOSPD2 and the recently described MOSPD1 and MOSPD3 are tether proteins of MCSs that are mainly found at the endoplasmic reticulum (ER). VAPs interact with various proteins with a motif called FFAT (two phenylalanines in an acidic tract), recruiting the associated organelle to the ER. In addition to the conventional FFAT motif, the recently described FFNT (two phenylal

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12

Hamamoto, Itsuki, Yorihiro Nishimura, Toru Okamoto, et al. "Human VAP-B Is Involved in Hepatitis C Virus Replication through Interaction with NS5A and NS5B." Journal of Virology 79, no. 21 (2005): 13473–82. http://dx.doi.org/10.1128/jvi.79.21.13473-13482.2005.

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ABSTRACT The hepatitis C virus (HCV) nonstructural protein (NS) 5A is a phosphoprotein that associates with various cellular proteins and participates in the replication of the HCV genome. Human vesicle-associated membrane protein-associated protein (VAP) subtype A (VAP-A) is known to be a host factor essential for HCV replication by binding to both NS5A and NS5B. To obtain more information on the NS5A protein in HCV replication, we screened human brain and liver libraries by a yeast two-hybrid system using NS5A as bait and identified VAP-B as an NS5A-binding protein. Immunoprecipitation and m

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Lapierre, L. A., P. L. Tuma, J. Navarre, J. R. Goldenring, and J. M. Anderson. "VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction." Journal of Cell Science 112, no. 21 (1999): 3723–32. http://dx.doi.org/10.1242/jcs.112.21.3723.

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Tight junctions create a regulated intercellular seal between epithelial and endothelial cells and also establish polarity between plasma membrane domains within the cell. Tight junctions have also been implicated in many other cellular functions, including cell signaling and growth regulation, but they have yet to be directly implicated in vesicle movement. Occludin is a transmembrane protein located at tight junctions and is known to interact with other tight junction proteins, including ZO-1. To investigate occludin's role in other cellular functions we performed a yeast two-hybrid screen u

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Venditti, Rossella, Laura Rita Rega, Maria Chiara Masone, et al. "Molecular determinants of ER–Golgi contacts identified through a new FRET–FLIM system." Journal of Cell Biology 218, no. 3 (2019): 1055–65. http://dx.doi.org/10.1083/jcb.201812020.

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ER–TGN contact sites (ERTGoCS) have been visualized by electron microscopy, but their location in the crowded perinuclear area has hampered their analysis via optical microscopy as well as their mechanistic study. To overcome these limits we developed a FRET-based approach and screened several candidates to search for molecular determinants of the ERTGoCS. These included the ER membrane proteins VAPA and VAPB and lipid transfer proteins possessing dual (ER and TGN) targeting motifs that have been hypothesized to contribute to the maintenance of ERTGoCS, such as the ceramide transfer protein CE

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15

Stanhope, Rebecca, and Isabelle Derré. "Making Contact: VAP Targeting by Intracellular Pathogens." Contact 1 (January 2018): 251525641877551. http://dx.doi.org/10.1177/2515256418775512.

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In naïve cells, the endoplasmic reticulum (ER) and the ER-resident Vesicle-associated membrane protein- Associated Proteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking of VAP by intracellular pathogens is a novel mechanism of host–pathogen interaction. Here, we summarize our recent findings showing that the Chlamydia inclusion membrane protein IncV tethers the ER to the inclusion membrane by binding to VAP via the molecular mimicry of two eukaryotic FFAT motifs.

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16

Kim, Yeun Ju, Maria Luisa Guzman-Hernandez, Eva Wisniewski, Nicolas Echeverria, and Tamas Balla. "Phosphatidylinositol and phosphatidic acid transport between the ER and plasma membrane during PLC activation requires the Nir2 protein." Biochemical Society Transactions 44, no. 1 (2016): 197–201. http://dx.doi.org/10.1042/bst20150187.

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Phospholipase C (PLC)-mediated hydrolysis of the limited pool of plasma membrane (PM) phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] requires replenishment from a larger pool of phosphatidylinositol (PtdIns) via sequential phosphorylation by PtdIns 4-kinases and phosphatidylinositol 4-phosphate (PtdIns4P) 5-kinases. Since PtdIns is synthesized in the endoplasmic reticulum (ER) and PtdIns(4,5)P2 is generated in the PM, it has been postulated that PtdIns transfer proteins (PITPs) provide the means for this lipid transfer function. Recent studies identified the large PITP protein, Nir2 as

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Slee, John A., and Timothy P. Levine. "Systematic Prediction of FFAT Motifs Across Eukaryote Proteomes Identifies Nucleolar and Eisosome Proteins With the Predicted Capacity to Form Bridges to the Endoplasmic Reticulum." Contact 2 (January 2019): 251525641988313. http://dx.doi.org/10.1177/2515256419883136.

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The endoplasmic reticulum (ER), the most pervasive organelle, exchanges information and material with many other organelles, but the extent of its interorganelle connections and the proteins that form bridges are not well known. The integral ER membrane protein vesicle-associated membrane protein-associated protein (VAP) is found in multiple bridges, interacting with many proteins that contain a short linear motif consisting of “two phenylalanines in an acidic tract” (FFAT). The VAP-FFAT interaction is the most common mechanism by which cytoplasmic proteins, particularly interorganelle bridges

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Aalto, Kristiina, Anu Autio, Elina A. Kiss, et al. "Siglec-9 is a novel leukocyte ligand for vascular adhesion protein-1 and can be used in PET imaging of inflammation and cancer." Blood 118, no. 13 (2011): 3725–33. http://dx.doi.org/10.1182/blood-2010-09-311076.

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Abstract Leukocyte migration to sites of inflammation is regulated by several endothelial adhesion molecules. Vascular adhesion protein-1 (VAP-1) is unique among the homing-associated molecules as it is both an enzyme that oxidizes primary amines and an adhesin. Although granulocytes can bind to endothelium via a VAP-1–dependent manner, the counter-receptor(s) on this leukocyte population is(are) not known. Here we used a phage display approach and identified Siglec-9 as a candidate ligand on granulocytes. The binding between Siglec-9 and VAP-1 was confirmed by in vitro and ex vivo adhesion as

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Borgese, Nica, Francesca Navone, Nobuyuki Nukina, and Tomoyuki Yamanaka. "Mutant VAPB: Culprit or Innocent Bystander of Amyotrophic Lateral Sclerosis?" Contact 4 (January 2021): 251525642110225. http://dx.doi.org/10.1177/25152564211022515.

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Nearly twenty years ago a mutation in the VAPB gene, resulting in a proline to serine substitution (p.P56S), was identified as the cause of a rare, slowly progressing, familial form of the motor neuron degenerative disease Amyotrophic Lateral Sclerosis (ALS). Since then, progress in unravelling the mechanistic basis of this mutation has proceeded in parallel with research on the VAP proteins and on their role in establishing membrane contact sites between the ER and other organelles. Analysis of the literature on cellular and animal models reviewed here supports the conclusion that P56S-VAPB,

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Kobayashi, Kappei, Seiji Tsuge, Livia Stavolone, and Thomas Hohn. "The Cauliflower Mosaic Virus Virion-Associated Protein Is Dispensable for Viral Replication in Single Cells." Journal of Virology 76, no. 18 (2002): 9457–64. http://dx.doi.org/10.1128/jvi.76.18.9457-9464.2002.

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ABSTRACT Cauliflower mosaic virus (CaMV) open reading frame III (ORF III) codes for a virion-associated protein (Vap), which is one of two viral proteins essential for aphid transmission. However, unlike the aphid transmission factor encoded by CaMV ORF II, Vap is also essential for systemic infection, suggesting that it is a multifunctional protein. To elucidate the additional function or functions of Vap, we tested the replication of noninfectious ORF III-defective mutants in transfected turnip protoplasts. PCR and Western blot analyses revealed that CaMV replication had occurred with an eff

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Soussan, Lior, Darya Burakov, Mathew P. Daniels, et al. "Erg30, a Vap-33–Related Protein, Functions in Protein Transport Mediated by Copi Vesicles." Journal of Cell Biology 146, no. 2 (1999): 301–12. http://dx.doi.org/10.1083/jcb.146.2.301.

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Intracellular transport of newly synthesized and mature proteins via vesicles is controlled by a large group of proteins. Here we describe a ubiquitous rat protein—endoplasmic reticulum (ER) and Golgi 30-kD protein (ERG30)—which shares structural characteristics with VAP-33, a 33-kD protein from Aplysia californica which was shown to interact with the synaptic protein VAMP. The transmembrane topology of the 30-kD ERG30 corresponds to a type II integral membrane protein, whose cytoplasmic NH2 terminus contains a predicted coiled-coil motif. We localized ERG30 to the ER and to pre-Golgi intermed

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Rocha, Nuno, Coenraad Kuijl, Rik van der Kant, et al. "Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7–RILP–p150Glued and late endosome positioning." Journal of Cell Biology 185, no. 7 (2009): 1209–25. http://dx.doi.org/10.1083/jcb.200811005.

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Late endosomes (LEs) have characteristic intracellular distributions determined by their interactions with various motor proteins. Motor proteins associated to the dynactin subunit p150Glued bind to LEs via the Rab7 effector Rab7-interacting lysosomal protein (RILP) in association with the oxysterol-binding protein ORP1L. We found that cholesterol levels in LEs are sensed by ORP1L and are lower in peripheral vesicles. Under low cholesterol conditions, ORP1L conformation induces the formation of endoplasmic reticulum (ER)–LE membrane contact sites. At these sites, the ER protein VAP (VAMP [vesi

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Wakana, Yuichi, Richika Kotake, Nanako Oyama, et al. "CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface." Molecular Biology of the Cell 26, no. 25 (2015): 4686–99. http://dx.doi.org/10.1091/mbc.e15-08-0599.

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Vesicle-associated membrane protein–associated protein (VAP) is an endoplasmic reticulum (ER)-resident integral membrane protein that controls a nonvesicular mode of ceramide and cholesterol transfer from the ER to the Golgi complex by interacting with ceramide transfer protein and oxysterol-binding protein (OSBP), respectively. We report that VAP and its interacting proteins are required for the processing and secretion of pancreatic adenocarcinoma up-regulated factor, whose transport from the trans-Golgi network (TGN) to the cell surface is mediated by transport carriers called “carriers of

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Borgese, Nica, Nicola Iacomino, Sara Francesca Colombo, and Francesca Navone. "The Link between VAPB Loss of Function and Amyotrophic Lateral Sclerosis." Cells 10, no. 8 (2021): 1865. http://dx.doi.org/10.3390/cells10081865.

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The VAP proteins are integral adaptor proteins of the endoplasmic reticulum (ER) membrane that recruit a myriad of interacting partners to the ER surface. Through these interactions, the VAPs mediate a large number of processes, notably the generation of membrane contact sites between the ER and essentially all other cellular membranes. In 2004, it was discovered that a mutation (p.P56S) in the VAPB paralogue causes a rare form of dominantly inherited familial amyotrophic lateral sclerosis (ALS8). The mutant protein is aggregation-prone, non-functional and unstable, and its expression from a s

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Chang, Shu-Jyuan, Hung-Pin Tu, Yen-Chang Clark Lai, et al. "Increased Vascular Adhesion Protein 1 (VAP-1) Levels Are Associated with Alternative M2 Macrophage Activation and Poor Prognosis for Human Gliomas." Diagnostics 10, no. 5 (2020): 256. http://dx.doi.org/10.3390/diagnostics10050256.

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Glioma is characterized by a high heterogeneity in the brain tumor. Abundant tumor-associated macrophages (TAMs) exist as neoplastic tissues, implicating tumor plasticity and thus leading to therapeutic challenges. Vascular adhesion protein (VAP-1) potentially serves as a mediator for TAM immunity in tumor milieu. We previously demonstrated that VAP-1 could contribute to tumor malignancy, but its characteristics in TAM immunity of glioma progression are still unclear. This study explored the association of VAP-1 expression with TAM distribution as well as the resulting clinical significance an

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Stavolone, Livia, Etienne Herzog, Denis Leclerc, and Thomas Hohn. "Tetramerization Is a Conserved Feature of the Virion-Associated Protein in Plant Pararetroviruses." Journal of Virology 75, no. 16 (2001): 7739–43. http://dx.doi.org/10.1128/jvi.75.16.7739-7743.2001.

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ABSTRACT All plant pararetroviruses belong to the Caulimoviridaefamily. This family contains six genera of viruses with different biological, serological, and molecular characteristics. Although some important mechanisms of viral replication and host infection are understood, much remains to be discovered about the many functions of the viral proteins. The focus of this study, the virion-associated protein (VAP), is conserved among all members of the group and contains a coiled-coil structure that has been shown to assemble as a tetramer in the case of cauliflower mosaic virus. We have used th

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Stanhope, Rebecca, Elizabeth Flora, Charlie Bayne, and Isabelle Derré. "IncV, a FFAT motif-containingChlamydiaprotein, tethers the endoplasmic reticulum to the pathogen-containing vacuole." Proceedings of the National Academy of Sciences 114, no. 45 (2017): 12039–44. http://dx.doi.org/10.1073/pnas.1709060114.

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Membrane contact sites (MCS) are zones of contact between the membranes of two organelles. At MCS, specific proteins tether the organelles in close proximity and mediate the nonvesicular trafficking of lipids and ions between the two organelles. The endoplasmic reticulum (ER) integral membrane protein VAP is a common component of MCS involved in both tethering and lipid transfer by binding directly to proteins containing a FFAT [two phenylalanines (FF) in an acidic tract (AT)] motif. In addition to maintaining cell homeostasis, MCS formation recently emerged as a mechanism by which intracellul

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Peretti, Diego, Nili Dahan, Eyal Shimoni, Koret Hirschberg, and Sima Lev. "Coordinated Lipid Transfer between the Endoplasmic Reticulum and the Golgi Complex Requires the VAP Proteins and Is Essential for Golgi-mediated Transport." Molecular Biology of the Cell 19, no. 9 (2008): 3871–84. http://dx.doi.org/10.1091/mbc.e08-05-0498.

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Lipid transport between intracellular organelles is mediated by vesicular and nonvesicular transport mechanisms and is critical for maintaining the identities of different cellular membranes. Nonvesicular lipid transport between the endoplasmic reticulum (ER) and the Golgi complex has been proposed to affect the lipid composition of the Golgi membranes. Here, we show that the integral ER–membrane proteins VAP-A and VAP-B affect the structural and functional integrity of the Golgi complex. Depletion of VAPs by RNA interference reduces the levels of phosphatidylinositol-4-phosphate (PI4P), diacy

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Geerds, Christina, Albert Haas, and Hartmut H. Niemann. "Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB." Acta Crystallographica Section F Structural Biology Communications 77, no. 8 (2021): 246–53. http://dx.doi.org/10.1107/s2053230x2100738x.

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Virulence-associated proteins (Vaps) contribute to the virulence of the pathogen Rhodococcus equi, but their mode of action has remained elusive. All Vaps share a conserved core of about 105 amino acids that folds into a compact eight-stranded antiparallel β-barrel with a unique topology. At the top of the barrel, four loops connect the eight β-strands. Previous Vap structures did not show concave surfaces that might serve as a ligand-binding site. Here, the structure of VapB in a new crystal form was determined at 1.71 Å resolution. The asymmetric unit contains two molecules. In one of them,

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Dorsch, Anna D., Julia E. Hölper, Kati Franzke, Luca M. Zaeck, Thomas C. Mettenleiter, and Barbara G. Klupp. "Role of Vesicle-Associated Membrane Protein-Associated Proteins (VAP) A and VAPB in Nuclear Egress of the Alphaherpesvirus Pseudorabies Virus." Viruses 13, no. 6 (2021): 1117. http://dx.doi.org/10.3390/v13061117.

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The molecular mechanism affecting translocation of newly synthesized herpesvirus nucleocapsids from the nucleus into the cytoplasm is still not fully understood. The viral nuclear egress complex (NEC) mediates budding at and scission from the inner nuclear membrane, but the NEC is not sufficient for efficient fusion of the primary virion envelope with the outer nuclear membrane. Since no other viral protein was found to be essential for this process, it was suggested that a cellular machinery is recruited by viral proteins. However, knowledge on fusion mechanisms involving the nuclear membrane

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Whittingham, Jean L., Elena V. Blagova, Ciaran E. Finn, et al. "Structure of the virulence-associated protein VapD from the intracellular pathogenRhodococcus equi." Acta Crystallographica Section D Biological Crystallography 70, no. 8 (2014): 2139–51. http://dx.doi.org/10.1107/s1399004714012632.

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Rhodococcus equiis a multi-host pathogen that infects a range of animals as well as immune-compromised humans. Equine and porcine isolates harbour a virulence plasmid encoding a homologous family of virulence-associated proteins associated with the capacity ofR. equito divert the normal processes of endosomal maturation, enabling bacterial survival and proliferation in alveolar macrophages. To provide a basis for probing the function of the Vap proteins in virulence, the crystal structure of VapD was determined. VapD is a monomer as determined by multi-angle laser light scattering. The structu

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Ettayebi, Khalil, and Michele E. Hardy. "Norwalk Virus Nonstructural Protein p48 Forms a Complex with the SNARE Regulator VAP-A and Prevents Cell Surface Expression of Vesicular Stomatitis Virus G Protein." Journal of Virology 77, no. 21 (2003): 11790–97. http://dx.doi.org/10.1128/jvi.77.21.11790-11797.2003.

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ABSTRACT Norwalk virus (NV), a reference strain of human calicivirus in the Norovirus genus of the family Caliciviridae, contains a positive-strand RNA genome with three open reading frames. ORF1 encodes a 1,789-amino-acid polyprotein that is processed into nonstructural proteins that include an NTPase, VPg, protease, and RNA-dependent RNA polymerase. The N-terminal protein p48 of ORF1 shows no significant sequence similarity to viral or cellular proteins, and its function in the human calicivirus replication cycle is not known. The lack of sequence similarity to any protein in the public data

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Zhu, Wenhe, Huiyan Wang, Wei Zhang, et al. "Protective effects and plausible mechanisms of antler-velvet polypeptide against hydrogen peroxide induced injury in human umbilical vein endothelial cells." Canadian Journal of Physiology and Pharmacology 95, no. 5 (2017): 610–19. http://dx.doi.org/10.1139/cjpp-2016-0196.

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Antler velvet polypeptide (VAP) is a prominent bioactive component of antler velvet. Whereas uncharacterized crude extracts have typically been used in pharmacological studies, in this study, the velvet polypeptide was isolated and purified by acid water extraction, ethanol precipitation, ammonium sulfate fractionation and precipitation, and chromatography, progressively. Human umbilical vein endothelial cells (HUVECs) were induced with H2O2 followed purified polypeptide treatment. Cell viability was evaluated by MTT assay. The apoptosis of cells was detected by fluorescence microscopy and flo

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Ernst, Wayne L., Kuntala Shome, Christine C. Wu, Xiaoyan Gong, Raymond A. Frizzell, and Meir Aridor. "VAMP-associated Proteins (VAP) as Receptors That Couple Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Proteostasis with Lipid Homeostasis." Journal of Biological Chemistry 291, no. 10 (2016): 5206–20. http://dx.doi.org/10.1074/jbc.m115.692749.

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Di Mattia, Thomas, Catherine Tomasetto, and Fabien Alpy. "A Third Musketeer on the ER: MOSPD2 is a Novel VAP-related Receptor for FFAT Motifs." Contact 1 (January 2018): 251525641880973. http://dx.doi.org/10.1177/2515256418809730.

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Interorganelle membrane contact sites are subcellular structures that favor exchange and communication inside the cell. Such microdomains are built by molecular bridges that create a physical connection between two distinct organelles. The field of contact sites is now flourishing with discoveries of new tethering molecules. In that context, we identified by an unbiased proteomic approach a novel scaffold protein named MOtile SPerm Domain-containing protein 2 (MOSPD2). MOSPD2 is an endoplasmic reticulum (ER)-resident protein that is able to interact with several organelle-bound proteins that p

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Corbeil, Denis, Mark F. Santos, Jana Karbanová, Thomas Kurth, Germana Rappa, and Aurelio Lorico. "Uptake and Fate of Extracellular Membrane Vesicles: Nucleoplasmic Reticulum-Associated Late Endosomes as a New Gate to Intercellular Communication." Cells 9, no. 9 (2020): 1931. http://dx.doi.org/10.3390/cells9091931.

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Extracellular membrane vesicles (EVs) are emerging as new vehicles in intercellular communication, but how the biological information contained in EVs is shared between cells remains elusive. Several mechanisms have been described to explain their release from donor cells and the initial step of their uptake by recipient cells, which triggers a cellular response. Yet, the intracellular routes and subcellular fate of EV content upon internalization remain poorly characterized. This is particularly true for EV-associated proteins and nucleic acids that shuttle to the nucleus of host cells. In th

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Miranda-CasoLuengo, Raúl, Aleksandra A. Miranda-CasoLuengo, Enda P. O’Connell, et al. "The vapA co-expressed virulence plasmid gene vcgB (orf10) of the intracellular actinomycete Rhodococcus equi." Microbiology 157, no. 8 (2011): 2357–68. http://dx.doi.org/10.1099/mic.0.049759-0.

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The virulence plasmid of the pathogenic actinomycete Rhodococcus equi is essential for proliferation of this pathogen in macrophages and the development of disease. The pathogenicity island of this plasmid encodes a family of virulence-associated proteins (Vap), one of which (VapA) is a virulence factor. This paper describes the vcgAB operon ( vapA co-expressed gene), located upstream of the vapA operon. Transcription of the vcgAB operon gave rise to transcripts with a half-life similar to those determined for other virulence plasmid genes (1.8 min). Transcription started at a promoter similar

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Inukai, Ryuta, Kanako Mori, Keiko Kuwata, et al. "The Novel ALG-2 Target Protein CDIP1 Promotes Cell Death by Interacting with ESCRT-I and VAPA/B." International Journal of Molecular Sciences 22, no. 3 (2021): 1175. http://dx.doi.org/10.3390/ijms22031175.

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Apoptosis-linked gene 2 (ALG-2, also known as PDCD6) is a member of the penta-EF-hand (PEF) family of Ca2+-binding proteins. The murine gene encoding ALG-2 was originally reported to be an essential gene for apoptosis. However, the role of ALG-2 in cell death pathways has remained elusive. In the present study, we found that cell death-inducing p53 target protein 1 (CDIP1), a pro-apoptotic protein, interacts with ALG-2 in a Ca2+-dependent manner. Co-immunoprecipitation analysis of GFP-fused CDIP1 (GFP-CDIP1) revealed that GFP-CDIP1 associates with tumor susceptibility gene 101 (TSG101), a know

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Matsuzaki, Fumiko, Michiko Shirane, Masaki Matsumoto, and Keiichi I. Nakayama. "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation." Molecular Biology of the Cell 22, no. 23 (2011): 4602–20. http://dx.doi.org/10.1091/mbc.e11-01-0068.

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Neurons are highly polarized cells with long neurites. Vesicular transport is required for neurite extension. We recently identified protrudin as a key regulator of vesicular transport during neurite extension. Expression of protrudin in nonneuronal cells thus induces formation of neurite-like membrane protrusions. We adopted a proteomics approach to identify proteins that associate with protrudin. Among the protrudin-associated proteins, including many with a function related to intracellular trafficking, we focused on KIF5, a motor protein that mediates anterograde vesicular transport in neu

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Ngo, Mike, and Neale D. Ridgway. "Oxysterol Binding Protein–related Protein 9 (ORP9) Is a Cholesterol Transfer Protein That Regulates Golgi Structure and Function." Molecular Biology of the Cell 20, no. 5 (2009): 1388–99. http://dx.doi.org/10.1091/mbc.e08-09-0905.

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Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) constitute a large gene family that differentially localize to organellar membranes, reflecting a functional role in sterol signaling and/or transport. OSBP partitions between the endoplasmic reticulum (ER) and Golgi apparatus where it imparts sterol-dependent regulation of ceramide transport and sphingomyelin synthesis. ORP9L also is localized to the ER–Golgi, but its role in secretion and lipid transport is unknown. Here we demonstrate that ORP9L partitioning between the trans-Golgi/trans-Golgi network (TGN), and the ER is med

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Li, Junyi, Chunling Xu, Sihua Yang, et al. "A Venom Allergen-Like Protein, RsVAP, the First Discovered Effector Protein of Radopholus similis That Inhibits Plant Defense and Facilitates Parasitism." International Journal of Molecular Sciences 22, no. 9 (2021): 4782. http://dx.doi.org/10.3390/ijms22094782.

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Radopholus similis is a migratory endoparasitic nematode that is extremely harmful to host plants. Venom allergen-like proteins (VAPs) are members of the cysteine-rich secretory protein family that are widely present in plants and animals. In this study, we cloned a VAP gene from R. similis, designated as RsVAP. RsVAP contains an open reading frame of 1089 bp encoding 362 amino acids. RsVAP is specifically expressed in the esophageal gland, and the expression levels of RsVAP are significantly higher in juveniles than in other life stages of R. similis. This expression pattern of RsVAP was cons

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Takai, Shinji, Stephen A. Hines, Tsutomu Sekizaki, et al. "DNA Sequence and Comparison of Virulence Plasmids from Rhodococcus equi ATCC 33701 and 103." Infection and Immunity 68, no. 12 (2000): 6840–47. http://dx.doi.org/10.1128/iai.68.12.6840-6847.2000.

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ABSTRACT The virulence plasmids of the equine virulent strainsRhodococcus equi ATCC 33701 and 103 were sequenced, and their genetic structure was analyzed. p33701 was 80,610 bp in length, and p103 was 1 bp shorter; their sequences were virtually identical. The plasmids contained 64 open reading frames (ORFs), 22 of which were homologous with genes of known function and 3 of which were homologous with putative genes of unknown function in other species. Putative functions were assigned to five ORFs based on protein family characteristics. The most striking feature of the virulence plasmids was

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Loewen, C. J. R. "A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP." EMBO Journal 22, no. 9 (2003): 2025–35. http://dx.doi.org/10.1093/emboj/cdg201.

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Kirmiz, Michael, Taryn E. Gillies, Eamonn J. Dickson, and James S. Trimmer. "Neuronal ER–plasma membrane junctions organized by Kv2–VAP pairing recruit Nir proteins and affect phosphoinositide homeostasis." Journal of Biological Chemistry 294, no. 47 (2019): 17735–57. http://dx.doi.org/10.1074/jbc.ra119.007635.

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Lin, Wenwu, Zhike Feng, K. Reddisiva Prasanth, Yuyan Liu, and Peter D. Nagy. "Dynamic interplay between the co-opted Fis1 mitochondrial fission protein and membrane contact site proteins in supporting tombusvirus replication." PLOS Pathogens 17, no. 3 (2021): e1009423. http://dx.doi.org/10.1371/journal.ppat.1009423.

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Plus-stranded RNA viruses have limited coding capacity and have to co-opt numerous pro-viral host factors to support their replication. Many of the co-opted host factors support the biogenesis of the viral replication compartments and the formation of viral replicase complexes on subverted subcellular membrane surfaces. Tomato bushy stunt virus (TBSV) exploits peroxisomal membranes, whereas the closely-related carnation Italian ringspot virus (CIRV) hijacks the outer membranes of mitochondria. How these organellar membranes can be recruited into pro-viral roles is not completely understood. He

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Foster, Leonard J., and Amira Klip. "Mechanism and regulation of GLUT-4 vesicle fusion in muscle and fat cells." American Journal of Physiology-Cell Physiology 279, no. 4 (2000): C877—C890. http://dx.doi.org/10.1152/ajpcell.2000.279.4.c877.

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Twenty years ago it was shown that recruitment of glucose transporters from an internal membrane compartment to the plasma membrane led to increased glucose uptake into fat and muscle cells stimulated by insulin. The final step of this process is the fusion of glucose transporter 4 (GLUT-4)-containing vesicles with the plasma membrane. The identification of a neuronal soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex as a requirement for synaptic vesicle-plasma membrane fusion led to the search for homologous complexes outside the nervous system. Indeed, iso

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Mitne-Neto, M., C. R. R. Ramos, D. C. Pimenta, et al. "A mutation in human VAP-B–MSP domain, present in ALS patients, affects the interaction with other cellular proteins." Protein Expression and Purification 55, no. 1 (2007): 139–46. http://dx.doi.org/10.1016/j.pep.2007.04.007.

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Barajas, Daniel, Kai Xu, Isabel Fernández de Castro Martín, et al. "Co-opted Oxysterol-Binding ORP and VAP Proteins Channel Sterols to RNA Virus Replication Sites via Membrane Contact Sites." PLoS Pathogens 10, no. 10 (2014): e1004388. http://dx.doi.org/10.1371/journal.ppat.1004388.

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Cooper, Charlotte R., Amanda J. Daugherty, Sabrina Tachdjian, Paul H. Blum, and Robert M. Kelly. "Role of vapBC toxin–antitoxin loci in the thermal stress response of Sulfolobus solfataricus." Biochemical Society Transactions 37, no. 1 (2009): 123–26. http://dx.doi.org/10.1042/bst0370123.

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TA (toxin–antitoxin) loci are ubiquitous in prokaryotic micro-organisms, including archaea, yet their physiological function is largely unknown. For example, preliminary reports have suggested that TA loci are microbial stress-response elements, although it was recently shown that knocking out all known chromosomally located TA loci in Escherichia coli did not have an impact on survival under certain types of stress. The hyperthermophilic crenarchaeon Sulfolobus solfataricus encodes at least 26 vapBC (where vap is virulence-associated protein) family TA loci in its genome. VapCs are PIN (PilT

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Loewen, Christopher J. R., and Timothy P. Levine. "A Highly Conserved Binding Site in Vesicle-associated Membrane Protein-associated Protein (VAP) for the FFAT Motif of Lipid-binding Proteins." Journal of Biological Chemistry 280, no. 14 (2005): 14097–104. http://dx.doi.org/10.1074/jbc.m500147200.

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