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  1. Article: Prix Nobel de médecine et physiologie 2013. Le trafic vésiculaire récompensé.

    Kuster, Aurélia / Galli, Thierry

    La Revue du praticien

    2014  Volume 64, Issue 2, Page(s) 175–177

    Title translation Nobel Prize in Physiology and Medicine 2013-the vesicular trafficking rewarded.
    MeSH term(s) Cell Membrane/physiology ; Humans ; Nobel Prize ; Transport Vesicles/physiology
    Language French
    Publishing date 2014-02
    Publishing country France
    Document type Journal Article
    ZDB-ID 205365-2
    ISSN 2101-017X ; 0035-2640
    ISSN (online) 2101-017X
    ISSN 0035-2640
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: ATG5 selectively engages virus-tethered BST2/tetherin in an LC3C-associated pathway.

    Judith, Delphine / Versapuech, Margaux / Bejjani, Fabienne / Palaric, Marjory / Verlhac, Pauline / Kuster, Aurelia / Lepont, Leslie / Gallois-Montbrun, Sarah / Janvier, Katy / Berlioz-Torrent, Clarisse

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 20, Page(s) e2217451120

    Abstract: Bone marrow stromal antigen 2 (BST2)/tetherin is a restriction factor that reduces HIV-1 dissemination by tethering virus at the cell surface. BST2 also acts as a sensor of HIV-1 budding, establishing a cellular antiviral state. The HIV-1 Vpu protein ... ...

    Abstract Bone marrow stromal antigen 2 (BST2)/tetherin is a restriction factor that reduces HIV-1 dissemination by tethering virus at the cell surface. BST2 also acts as a sensor of HIV-1 budding, establishing a cellular antiviral state. The HIV-1 Vpu protein antagonizes BST2 antiviral functions via multiple mechanisms, including the subversion of an LC3C-associated pathway, a key cell intrinsic antimicrobial mechanism. Here, we describe the first step of this viral-induced LC3C-associated process. This process is initiated at the plasma membrane through the recognition and internalization of virus-tethered BST2 by ATG5, an autophagy protein. ATG5 and BST2 assemble as a complex, independently of the viral protein Vpu and ahead of the recruitment of the ATG protein LC3C. The conjugation of ATG5 with ATG12 is dispensable for this interaction. ATG5 recognizes cysteine-linked homodimerized BST2 and specifically engages phosphorylated BST2 tethering viruses at the plasma membrane, in an LC3C-associated pathway. We also found that this LC3C-associated pathway is used by Vpu to attenuate the inflammatory responses mediated by virion retention. Overall, we highlight that by targeting BST2 tethering viruses, ATG5 acts as a signaling scaffold to trigger an LC3C-associated pathway induced by HIV-1 infection.
    MeSH term(s) Antiviral Agents/metabolism ; Bone Marrow Stromal Antigen 2 ; Cell Membrane/metabolism ; GPI-Linked Proteins/genetics ; GPI-Linked Proteins/metabolism ; Human Immunodeficiency Virus Proteins/genetics ; Human Immunodeficiency Virus Proteins/metabolism ; Viral Proteins/metabolism ; Viral Regulatory and Accessory Proteins/genetics ; Viral Regulatory and Accessory Proteins/metabolism ; Viruses/metabolism ; Humans
    Chemical Substances Antiviral Agents ; Bone Marrow Stromal Antigen 2 ; GPI-Linked Proteins ; Human Immunodeficiency Virus Proteins ; Viral Proteins ; Viral Regulatory and Accessory Proteins ; ATG5 protein, human ; MAP1LC3C protein, human
    Language English
    Publishing date 2023-05-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2217451120
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Surgical site infections after kidney transplantation are independently associated with graft loss.

    Schreiber, Peter W / Hoessly, Linard D / Boggian, Katia / Neofytos, Dionysios / van Delden, Christian / Egli, Adrian / Dickenmann, Michael / Hirzel, Cédric / Manuel, Oriol / Koller, Michael / Rossi, Simona / Banz, Vanessa / Schmied, Bruno / Guerke, Lorenz / Matter, Maurice / de Rougemont, Olivier / Bonani, Marco / Golshayan, Déla / Schnyder, Aurelia /
    Sidler, Daniel / Haidar, Fadi / Kuster, Stefan P / Stampf, Susanne / Mueller, Nicolas J

    American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons

    2023  

    Abstract: Surgical site infections (SSIs) are common health care-associated infections. SSIs after kidney transplantation (K-Tx) can endanger patient and allograft survival. Multicenter studies on this early posttransplant complication are scarce. We analyzed ... ...

    Abstract Surgical site infections (SSIs) are common health care-associated infections. SSIs after kidney transplantation (K-Tx) can endanger patient and allograft survival. Multicenter studies on this early posttransplant complication are scarce. We analyzed consecutive adult K-Tx recipients enrolled in the Swiss Transplant Cohort Study who received a K-Tx between May 2008 and September 2020. All data were prospectively collected with the exception of the categorization of SSI which was performed retrospectively according to the Centers for Disease Control and Prevention criteria. A total of 58 out of 3059 (1.9%) K-Tx recipients were affected by SSIs. Deep incisional (15, 25.9%) and organ/space infections (34, 58.6%) predominated. In the majority of SSIs (52, 89.6%), bacteria were detected, most frequently Escherichia coli (15, 28.9%), Enterococcus spp. (14, 26.9%), and coagulase-negative staphylococci (13, 25.0%). A BMI ≥25 kg/m
    Language English
    Publishing date 2023-11-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2060594-8
    ISSN 1600-6143 ; 1600-6135
    ISSN (online) 1600-6143
    ISSN 1600-6135
    DOI 10.1016/j.ajt.2023.11.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Une récompense pour la découverte des acteurs et des mécanismes moléculaires fondamentaux du trafic vésiculaire intracellulaire - Prix Nobel de Médecine 2013 James Rothman, Randy Schekman et Thomas Südhof.

    Galli, Thierry / Kuster, Aurélia / Tareste, David

    Medecine sciences : M/S

    2013  Volume 29, Issue 11, Page(s) 1055–1058

    Title translation Nobel Prize in Physiology and Medicine 2013 - an award for the discovery of the actors and fundamental molecular mechanisms of intracellular vesicle trafficking.
    MeSH term(s) Biological Transport ; Cell Physiological Phenomena ; Exocytosis ; Germany ; History, 20th Century ; History, 21st Century ; Intracellular Membranes/physiology ; Membrane Fusion ; Neurotransmitter Agents/metabolism ; Nobel Prize ; Physiology ; SNARE Proteins ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/ultrastructure ; Synaptic Transmission ; United States
    Chemical Substances Neurotransmitter Agents ; SNARE Proteins
    Language French
    Publishing date 2013-11
    Publishing country France
    Document type Biography ; Historical Article ; Journal Article
    ZDB-ID 632733-3
    ISSN 1958-5381 ; 0767-0974
    ISSN (online) 1958-5381
    ISSN 0767-0974
    DOI 10.1051/medsci/20112713024
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.B 2872: Show issues Location:
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  5. Article ; Online: LC3C Contributes to Vpu-Mediated Antagonism of BST2/Tetherin Restriction on HIV-1 Release through a Non-canonical Autophagy Pathway.

    Madjo, Ursula / Leymarie, Olivier / Frémont, Stéphane / Kuster, Aurelia / Nehlich, Mélanie / Gallois-Montbrun, Sarah / Janvier, Katy / Berlioz-Torrent, Clarisse

    Cell reports

    2016  Volume 17, Issue 9, Page(s) 2221–2233

    Abstract: BST2 (bone marrow stromal antigen 2)/tetherin is a restriction factor of enveloped viruses, which blocks the release of viral particles. HIV-1 encodes proteins that antagonize this innate barrier, including the accessory protein Vpu. Here, we investigate ...

    Abstract BST2 (bone marrow stromal antigen 2)/tetherin is a restriction factor of enveloped viruses, which blocks the release of viral particles. HIV-1 encodes proteins that antagonize this innate barrier, including the accessory protein Vpu. Here, we investigate whether the autophagy pathway and/or ATG proteins are hijacked by HIV-1 Vpu to circumvent BST2 restriction of viral release. We report that BST2 and Vpu are present in LC3-positive compartments. We found that Vpu selectively interacts with the ATG8 ortholog LC3C through the Vpu L
    Language English
    Publishing date 2016-11-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2016.10.045
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The Q-soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor (Q-SNARE) SNAP-47 Regulates Trafficking of Selected Vesicle-associated Membrane Proteins (VAMPs).

    Kuster, Aurelia / Nola, Sebastien / Dingli, Florent / Vacca, Barbara / Gauchy, Christian / Beaujouan, Jean-Claude / Nunez, Marcela / Moncion, Thomas / Loew, Damarys / Formstecher, Etienne / Galli, Thierry / Proux-Gillardeaux, Veronique

    The Journal of biological chemistry

    2015  Volume 290, Issue 47, Page(s) 28056–28069

    Abstract: SNAREs constitute the core machinery of intracellular membrane fusion, but vesicular SNAREs localize to specific compartments via largely unknown mechanisms. Here, we identified an interaction between VAMP7 and SNAP-47 using a proteomics approach. We ... ...

    Abstract SNAREs constitute the core machinery of intracellular membrane fusion, but vesicular SNAREs localize to specific compartments via largely unknown mechanisms. Here, we identified an interaction between VAMP7 and SNAP-47 using a proteomics approach. We found that SNAP-47 mainly localized to cytoplasm, the endoplasmic reticulum (ER), and ERGIC and could also shuttle between the cytoplasm and the nucleus. SNAP-47 preferentially interacted with the trans-Golgi network VAMP4 and post-Golgi VAMP7 and -8. SNAP-47 also interacted with ER and Golgi syntaxin 5 and with syntaxin 1 in the absence of Munc18a, when syntaxin 1 is retained in the ER. A C-terminally truncated SNAP-47 was impaired in interaction with VAMPs and affected their subcellular distribution. SNAP-47 silencing further shifted the subcellular localization of VAMP4 from the Golgi apparatus to the ER. WT and mutant SNAP-47 overexpression impaired VAMP7 exocytic activity. We conclude that SNAP-47 plays a role in the proper localization and function of a subset of VAMPs likely via regulation of their transport through the early secretory pathway.
    MeSH term(s) Animals ; Dogs ; Madin Darby Canine Kidney Cells ; Protein Transport ; Q-SNARE Proteins/physiology ; R-SNARE Proteins/metabolism ; Subcellular Fractions/metabolism
    Chemical Substances Q-SNARE Proteins ; R-SNARE Proteins
    Language English
    Publishing date 2015-09-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M115.666362
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Increased activity of the vesicular soluble N-ethylmaleimide-sensitive factor attachment protein receptor TI-VAMP/VAMP7 by tyrosine phosphorylation in the Longin domain.

    Burgo, Andrea / Casano, Alessandra M / Kuster, Aurelia / Arold, Stefan T / Wang, Guan / Nola, Sébastien / Verraes, Agathe / Dingli, Florent / Loew, Damarys / Galli, Thierry

    The Journal of biological chemistry

    2013  Volume 288, Issue 17, Page(s) 11960–11972

    Abstract: Vesicular (v)- and target (t)-SNAREs play essential roles in intracellular membrane fusion through the formation of cytoplasmic α-helical bundles. Several v-SNAREs have a Longin N-terminal extension that, by promoting a closed conformation, plays an ... ...

    Abstract Vesicular (v)- and target (t)-SNAREs play essential roles in intracellular membrane fusion through the formation of cytoplasmic α-helical bundles. Several v-SNAREs have a Longin N-terminal extension that, by promoting a closed conformation, plays an autoinhibitory function and decreases SNARE complex formation and membrane fusion efficiency. The molecular mechanism leading to Longin v-SNARE activation is largely unknown. Here we find that exocytosis mediated by the Longin v-SNARE TI-VAMP/VAMP7 is activated by tonic treatment with insulin and insulin-like growth factor-1 but not by depolarization and intracellular calcium rise. In search of a potential downstream mechanism, we found that TI-VAMP is phosphorylated in vitro by c-Src kinase on tyrosine 45 of the Longin domain. Accordingly, a mutation of tyrosine 45 into glutamate, but not phenylalanine, activates both t-SNARE binding and exocytosis. Activation of TI-VAMP-mediated exocytosis thus relies on tyrosine phosphorylation.
    MeSH term(s) Animals ; COS Cells ; CSK Tyrosine-Protein Kinase ; Chlorocebus aethiops ; Exocytosis/drug effects ; Exocytosis/physiology ; HeLa Cells ; Humans ; Hypoglycemic Agents/pharmacology ; Insulin/pharmacology ; Insulin-Like Growth Factor I/pharmacology ; Phosphorylation/physiology ; Protein Structure, Tertiary ; R-SNARE Proteins/genetics ; R-SNARE Proteins/metabolism ; SNARE Proteins/genetics ; SNARE Proteins/metabolism ; src-Family Kinases/genetics ; src-Family Kinases/metabolism
    Chemical Substances Hypoglycemic Agents ; Insulin ; R-SNARE Proteins ; SNARE Proteins ; VAMP7 protein, human ; Insulin-Like Growth Factor I (67763-96-6) ; CSK Tyrosine-Protein Kinase (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2) ; CSK protein, human (EC 2.7.10.23)
    Language English
    Publishing date 2013-03-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M112.415075
    Database MEDical Literature Analysis and Retrieval System OnLINE

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