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687 results on '"Golgi membrane"'

6. Arabidopsis PLDζ1 and PLDζ2 localize to post-Golgi membrane compartments in a partially overlapping manner

Author

Yukimi Yamamoto Taniguchi, Takashi Aoyama, Yohei Ohashi, Ryota Shimamura, Mariko Kato, and Tomohiko Tsuge

Subjects
Arabidopsis, Golgi Apparatus, Plant Science, Vacuole, Real-Time Polymerase Chain Reaction, Plant Roots, Gravitropism, symbols.namesake, Phospholipase D, Genetics, Arabidopsis thaliana, Golgi membrane, Microscopy, Confocal, biology, Arabidopsis Proteins, General Medicine, Golgi apparatus, Plants, Genetically Modified, Subcellular localization, biology.organism_classification, Cell biology, symbols, Signal transduction, Agronomy and Crop Science
Abstract

Arabidopsis PLDζ1 and PLDζ2 localize to the trans-Golgi network and to compartments including the trans-Golgi network, multi-vesicular bodies, and the tonoplast, respectively, depending on their N-terminal regions containing PX-PH domains. Phospholipase D (PLD) is involved in dynamic cellular processes, including membrane trafficking, cytoskeletal reorganization, and signal transduction for gene expression, through the production of phosphatidic acid in membrane compartments specific to each process. Although PLD plays crucial roles in various plant phenomena, the underlying processes involving PLD for each phenomenon remain largely elusive, partly because the subcellular localization of PLD remains obscure. In this study, we performed comparative subcellular localization analyses of the Arabidopsis thaliana PX-PH-PLDs PLDζ1 and PLDζ2. In mature lateral root cap cells, own promoter-driven fluorescence protein fusions of PLDζ1 localized to the entire trans-Golgi network (TGN) while that of PLDζ2 localized to punctate structures including part of the TGN and multi-vesicular bodies as well as the tonoplast. These localization patterns were reproduced using N-terminal partial proteins, which contain PX-PH domains. An inducibly overexpressed fluorescence protein fusion of the PLDζ2 partial protein first localized to punctate structures, and then accumulated predominantly on the tonoplast. Further domain dissection analysis revealed that the N-terminal moiety preceding the PX-PH domain of PLDζ2 was required for the tonoplast-predominant accumulation. These findings suggest that PLDζ1 and PLDζ2 play partially overlapping but nonetheless distinctive roles in post-Golgi compartments along the membrane trafficking pathway from the TGN to the tonoplast.

Published
2021
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16. SNAREs

Author

Banfield, David K., Hong, Wanjin, Mironov, Alexander A., editor, and Pavelka, Margit, editor

Published
2008
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31. Arf and Phospholipids

Author

Randazzo, Paul A., Nie, Zhongzhen, Hirsch, Dianne S., Ridley, Anne, editor, Frampton, Jon, editor, and Kahn, Richard A.

Published
2003
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37. Coat Proteins

Author

Boman, Annette, Nilsson, Tommy, Ridley, Anne, editor, Frampton, Jon, editor, and Kahn, Richard A.

Published
2003
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40. β4-Galactosyltransferase-I

Author

Shaper, Nancy L., Shaper, Joel H., Taniguchi, Naoyuki, editor, Honke, Koichi, editor, Fukuda, Minoru, editor, Clausen, Henrik, editor, Furukawa, Kiyoshi, editor, Hart, Gerald W., editor, Kannagi, Reiji, editor, Kawasaki, Toshisuke, editor, Kinoshita, Taroh, editor, Muramatsu, Takashi, editor, Saito, Masaki, editor, Shaper, Joel H., editor, Sugahara, Kazuyuki, editor, Tabak, Lawrence A., editor, Van den Eijnden, Dirk H., editor, Yanagishita, Masaki, editor, Dennis, James W., editor, Furukawa, Koichi, editor, Hirabayashi, Yoshio, editor, Kawakita, Masao, editor, Kimata, Koji, editor, Lindahl, Ulf, editor, Narimatsu, Hisashi, editor, Schachter, Harry, editor, Stanley, Pamela, editor, Suzuki, Akemi, editor, Tsuji, Shuichi, editor, and Yamashita, Katsuko, editor

Published
2002
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41. UDP-Gal Transporter-1 and -2

Author

Kawakita, Masao, Ishida, Nobuhiro, Taniguchi, Naoyuki, editor, Honke, Koichi, editor, Fukuda, Minoru, editor, Clausen, Henrik, editor, Furukawa, Kiyoshi, editor, Hart, Gerald W., editor, Kannagi, Reiji, editor, Kawasaki, Toshisuke, editor, Kinoshita, Taroh, editor, Muramatsu, Takashi, editor, Saito, Masaki, editor, Shaper, Joel H., editor, Sugahara, Kazuyuki, editor, Tabak, Lawrence A., editor, Van den Eijnden, Dirk H., editor, Yanagishita, Masaki, editor, Dennis, James W., editor, Furukawa, Koichi, editor, Hirabayashi, Yoshio, editor, Kawakita, Masao, editor, Kimata, Koji, editor, Lindahl, Ulf, editor, Narimatsu, Hisashi, editor, Schachter, Harry, editor, Stanley, Pamela, editor, Suzuki, Akemi, editor, Tsuji, Shuichi, editor, and Yamashita, Katsuko, editor

Published
2002
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42. UDP-GlcNAc Transporter

Author

Kawakita, Masao, Ishida, Nobuhiro, Taniguchi, Naoyuki, editor, Honke, Koichi, editor, Fukuda, Minoru, editor, Clausen, Henrik, editor, Furukawa, Kiyoshi, editor, Hart, Gerald W., editor, Kannagi, Reiji, editor, Kawasaki, Toshisuke, editor, Kinoshita, Taroh, editor, Muramatsu, Takashi, editor, Saito, Masaki, editor, Shaper, Joel H., editor, Sugahara, Kazuyuki, editor, Tabak, Lawrence A., editor, Van den Eijnden, Dirk H., editor, Yanagishita, Masaki, editor, Dennis, James W., editor, Furukawa, Koichi, editor, Hirabayashi, Yoshio, editor, Kawakita, Masao, editor, Kimata, Koji, editor, Lindahl, Ulf, editor, Narimatsu, Hisashi, editor, Schachter, Harry, editor, Stanley, Pamela, editor, Suzuki, Akemi, editor, Tsuji, Shuichi, editor, and Yamashita, Katsuko, editor

Published
2002
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43. CMP-Sialic Acid Transporter

Author

Gerardy-Schahn, Rita, Taniguchi, Naoyuki, editor, Honke, Koichi, editor, Fukuda, Minoru, editor, Clausen, Henrik, editor, Furukawa, Kiyoshi, editor, Hart, Gerald W., editor, Kannagi, Reiji, editor, Kawasaki, Toshisuke, editor, Kinoshita, Taroh, editor, Muramatsu, Takashi, editor, Saito, Masaki, editor, Shaper, Joel H., editor, Sugahara, Kazuyuki, editor, Tabak, Lawrence A., editor, Van den Eijnden, Dirk H., editor, Yanagishita, Masaki, editor, Dennis, James W., editor, Furukawa, Koichi, editor, Hirabayashi, Yoshio, editor, Kawakita, Masao, editor, Kimata, Koji, editor, Lindahl, Ulf, editor, Narimatsu, Hisashi, editor, Schachter, Harry, editor, Stanley, Pamela, editor, Suzuki, Akemi, editor, Tsuji, Shuichi, editor, and Yamashita, Katsuko, editor

Published
2002
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44. GlcCer Synthase (UDP-Glucose:Ceramide Glucosyltransferase, UGCG)

Author

Hirabayashi, Yoshio, Ichikawa, Shinichi, Taniguchi, Naoyuki, editor, Honke, Koichi, editor, Fukuda, Minoru, editor, Clausen, Henrik, editor, Furukawa, Kiyoshi, editor, Hart, Gerald W., editor, Kannagi, Reiji, editor, Kawasaki, Toshisuke, editor, Kinoshita, Taroh, editor, Muramatsu, Takashi, editor, Saito, Masaki, editor, Shaper, Joel H., editor, Sugahara, Kazuyuki, editor, Tabak, Lawrence A., editor, Van den Eijnden, Dirk H., editor, Yanagishita, Masaki, editor, Dennis, James W., editor, Furukawa, Koichi, editor, Hirabayashi, Yoshio, editor, Kawakita, Masao, editor, Kimata, Koji, editor, Lindahl, Ulf, editor, Narimatsu, Hisashi, editor, Schachter, Harry, editor, Stanley, Pamela, editor, Suzuki, Akemi, editor, Tsuji, Shuichi, editor, and Yamashita, Katsuko, editor

Published
2002
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45. Investigation of the Role of Protein Kinase D in Human Rhinovirus Replication.

Author

Guedán, Anabel, Swieboda, Dawid, Charles, Mark, Toussaint, Marie, Johnston, Sebastian L., Asfor, Amin, Panjwani, Anusha, Tuthill, Tobias J., Danahay, Henry, Raynham, Tony, Mousnier, Aurelie, and Solari, Roberto

Subjects
*PROTEIN kinases, *PICORNAVIRUSES, *RHINOVIRUSES, *VIRAL replication, *ENDOPLASMIC reticulum
Abstract

Picornavirus replication is known to cause extensive remodeling of Golgi and endoplasmic reticulum membranes, and a number of the host proteins involved in the viral replication complex have been identified, including oxysterol binding protein (OSBP) and phosphatidylinositol 4-kinase III beta (PI4KB). Since both OSBP and PI4KB are substrates for protein kinase D (PKD) and PKD is known to be involved in the control of Golgi membrane vesicular and lipid transport, we hypothesized that PKD played a role in viral replication. We present multiple lines of evidence in support of this hypothesis. First, infection of HeLa cells with human rhinovirus (HRV) induced the phosphorylation of PKD. Second, PKD inhibitors reduced HRV genome replication, protein expression, and titers in a concentrationdependent fashion and also blocked the replication of poliovirus (PV) and foot-and-mouth disease virus (FMDV) in a variety of cells. Third, HRV replication was significantly reduced in HeLa cells overexpressing wild-type and mutant forms of PKD1. Fourth, HRV genome replication was reduced in HAP1 cells in which the PKD1 gene was knocked out by clustered regularly interspaced short palindromic repeats (CRISPR)-Cas9. Although we have not identified the molecular mechanism through which PKD regulates viral replication, our data suggest that this is not due to enhanced interferon signaling or an inhibition of clathrin-mediated endocytosis, and PKD inhibitors do not need to be present during viral uptake. Our data show for the first time that targeting PKD with small molecules can inhibit the replication of HRV, PV, and FMDV, and therefore, PKD may represent a novel antiviral target for drug discovery. [ABSTRACT FROM AUTHOR]

Published
2017
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47. COVID-19: Update on Pathogenesis and Treatment Strategies

Author

Shikha Srivastava, Rakesh Kumar Chauhan, and Pankaj Sharma

Subjects
Golgi membrane, biology, medicine.drug_class, business.industry, viruses, Endoplasmic reticulum, Immunology, Lipid bilayer fusion, Monoclonal antibody, medicine.disease_cause, Virology, Virus, Pathogenesis, medicine, biology.protein, Immunology and Allergy, Antibody, business, Coronavirus
Abstract

COVID-19 (Coronavirus disease) is the most contagious virus, which has been characterized as a global pandemic by WHO. The pathological cycle of COVID-19 virus can be specified as RNAaemia, severe pneumonia, along with the Ground-glass opacity (GGO), and acute cardiac injury. The S protein of Coronavirus has been reported to be involved in the entry of the virus into the host cell, which can be accomplished by direct membrane fusion between the virus and plasma membrane. In the endoplasmic reticulum or Golgi membrane, the newly formed enveloped glycoproteins are introduced. The spread of disease occurs due to contact and droplets unleashed by the vesicles holding the virus particles combined with the plasma membrane to the virus released by the host. The present manuscript describes the pathogenesis of COVID-19 and various treatment strategies that include drugs such as chloroquine and hydroxychloroquine, an anti-malarial drug, antibodies: SARS-CoV-specific human monoclonal antibody CR3022 and plasma treatment facilitate the therapeutic effect.

Published
2020
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48. Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment

Author

Lin Feng, Hui-Ping He, Xiao Zhang, Bing Yu, Miao Xu, Yu-Xin Lin, Luo Meng, Mu Sheng Zeng, Xiaoxue Chen, Jun-Ying Ou, Song Gao, Hua Zhang, Yu-Lu Cao, and Yi Xin Zeng

Subjects
0301 basic medicine, Protein Conformation, alpha-Helical, Epstein-Barr Virus Infections, Herpesvirus 4, Human, viruses, Science, 030106 microbiology, General Physics and Astronomy, Plasma protein binding, Genome, Viral, medicine.disease_cause, General Biochemistry, Genetics and Molecular Biology, Article, Peptide nucleic acid oligo, 03 medical and health sciences, symbols.namesake, Protein structure, Capsid, hemic and lymphatic diseases, medicine, Humans, Herpes virus, lcsh:Science, X-ray crystallography, chemistry.chemical_classification, Golgi membrane, Multidisciplinary, General Chemistry, Viral tegument, Golgi apparatus, Epstein–Barr virus, Cell biology, 030104 developmental biology, chemistry, symbols, lcsh:Q, Glycoprotein, Protein Binding
Abstract

Epstein-Barr virus (EBV) is a γ-herpesvirus associated with the occurrence of several human malignancies. BBRF2 and BSRF1 are two EBV tegument proteins that have been suggested to form a hetero-complex and mediate viral envelopment, but the molecular basis of their interaction and the functional mechanism of this complex remains unknown. Here, we present crystal structures of BBRF2 alone and in complex with BSRF1. BBRF2 has a compact globular architecture featuring a central β-sheet that is surrounded by 10 helices, it represents a novel fold distinct from other known protein structures. The central portion of BSRF1 folds into two tightly associated antiparallel α-helices, forming a composite four-helix bundle with two α-helices from BBRF2 via a massive hydrophobic network. In vitro, a BSRF1-derived peptide binds to BBRF2 and reduces the number of viral genome copies in EBV-positive cells. Exogenous BBRF2 and BSRF1 co-localize at the Golgi apparatus. Furthermore, BBRF2 binds capsid and capsid-associated proteins, whereas BSRF1 associates with glycoproteins. These findings indicate that the BBRF2-BSRF1 complex tethers EBV nucleocapsids to the glycoprotein-enriched Golgi membrane, facilitating secondary envelopment., Epstein-Barr virus (EBV) tegument proteins BBRF2 and BSRF1 have been suggested to form a hetero-complex. Here, He et al. provide the crystal structures of BBRF2 alone and in complex with BSRF1 and suggest that the complex tethers EBV nucleocapsids to the Golgi membrane, facilitating secondary envelopment.

Published
2020

49. Rab35 Targeting to the Plasma Membrane Is Dependent on the C-terminal Polybasic Cluster

Author

Youhei Egami, Katsuhisa Kawai, Arata Nishigaki, and Nobukazu Araki

Subjects
chemistry.chemical_classification, basic clusters, Golgi membrane, Histology, Physiology, Chemistry, C-terminus, Cell Biology, GTPase, Note, plasma membrane, confocal microscopy, Subcellular localization, Biochemistry, Pathology and Forensic Medicine, Cell biology, Amino acid, law.invention, Membrane, Rab35, Confocal microscopy, law, Rab
Abstract

Rab35, a member of the Rab GTPase family, has been implicated in various cellular processes including cell motility and membrane trafficking. Although Rab35 is localized to the plasma membrane, Rab proteins that are identified to have high sequence homology with Rab35 exhibit distinct subcellular localization patterns. Comparing the amino acid sequences between Rab35 and its family members revealed a significant variation in an approximate 30-amino acid region of the C-terminus. This suggests that this region determines the subcellular localization of individual Rab proteins. To confirm this hypothesis, we constructed Rab35–Rab10 chimera proteins by exchanging their C-terminal domains with one another. Confocal microscopy of RAW264 cells expressing EGFP-fused Rab35–Rab10 chimeras has indicated that the C-terminal region of Rab35 is critical for its plasma membrane localization. Furthermore, we were able to determine that a basic amino acid cluster exists in the C-terminal region of Rab35 and that Rab35 localization shifts to the Golgi membrane when the number of basic amino acids in this region is reduced. Thus, it is likely that the approximate 30-amino acid C-terminal region containing basic clusters is responsible for Rab35 plasma membrane localization and that its preferential localization depends on the number of basic amino acids.

Published
2020
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50. Function of Arl4aa in the Initiation of Hematopoiesis in Zebrafish by Maintaining Golgi Complex Integrity in Hemogenic Endothelium

Author

Bai-Liang He, Alvin C.H. Ma, May P.L. Cheung, Toni K. Man, Nelson K. L. Ng, Yuhan Guo, Dandan Wang, Xiangguo Shi, Anskar Y.H. Leung, and Bowie Yik Ling Cheng

Subjects
definitive hematopoietic stem cells, 0301 basic medicine, Hemangioblasts, Notch signaling pathway, Down-Regulation, Golgi Apparatus, Models, Biological, Biochemistry, Article, 03 medical and health sciences, symbols.namesake, 0302 clinical medicine, Transcription Activator-Like Effector Nucleases, Genetics, Animals, Humans, Zebrafish, Notch signaling, Conserved Sequence, Crosses, Genetic, Hemogenic endothelium, Golgi membrane, Gene knockdown, Base Sequence, Receptors, Notch, biology, Hematopoietic Tissue, Endothelial Cells, Cell Biology, Zebrafish Proteins, Golgi apparatus, zebrafish, biology.organism_classification, Golgi complex, Hematopoiesis, Cell biology, 030104 developmental biology, Mutation, symbols, Arl4aa, Stem cell, 030217 neurology & neurosurgery, Signal Transduction, Developmental Biology
Abstract

Summary ADP-ribosylation factor-like 4aa (Arl4aa) is a member of the ADP-ribosylation factor family. It is expressed in hematopoietic tissue during embryonic development, but its function was unknown. Zebrafish arl4aa is preferentially expressed in the ventral wall of the dorsal aorta (VDA) at 24 and 36 hpf and in caudal hematopoietic tissue at 48 hpf. Morpholino knockdown and transcription activator-like effector nuclease (TALEN) knockout of arl4aa significantly reduced expression of genes associated with definitive hematopoietic stem cells (HSCs). Golgi complex integrity in VDA was disrupted as shown by transmission electron microscopy and immunostaining of Golgi membrane Giantin. Mechanistically, arl4aa knockdown reduced Notch signaling in the VDA and its target gene expression. Protein expression of NICD was also reduced. Effects of arl4aa knockdown on definitive hematopoiesis could be restored by NICD expression. This study identified arl4aa as a factor regulating initiation of definitive HSCs by maintaining the integrity of Golgi complex and, secondarily, maturation of the Notch receptor., Highlights • arl4aa expressed in ventral wall of dorsal aorta and caudal hematopoietic tissue • arl4aa maintained Golgi complex integrity and Notch signaling in definitive HSCs • Deletion of arl4aa perturbed initiation of definitive HSCs, In this study, Anskar Y.H. Leung and colleagues show that arl4aa was expressed in the ventral wall of the dorsal aorta and caudal hematopoietic tissue during zebrafish embryo development. Deletion of arl4aa disrupted the integrity of the Golgi complex and Notch signaling and perturbed derivation of definitive hematopoietic stem cells from hemogenic endothelium. arl4aa might emerge as a regulator of embryonic hematopoiesis.

Published
2020
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