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  1. Article ; Online: The NEDD4 ubiquitin E3 ligase: a snapshot view of its functional activity and regulation.

    Sicari, Daria / Weber, Janine / Maspero, Elena / Polo, Simona

    Biochemical Society transactions

    2021  Volume 50, Issue 1, Page(s) 473–485

    Abstract: Due to its fundamental role in all eukaryotic cells, a deeper understanding of the molecular mechanisms underlying ubiquitination is of central importance. Being responsible for chain specificity and substrate recognition, E3 ligases are the selective ... ...

    Abstract Due to its fundamental role in all eukaryotic cells, a deeper understanding of the molecular mechanisms underlying ubiquitination is of central importance. Being responsible for chain specificity and substrate recognition, E3 ligases are the selective elements of the ubiquitination process. In this review, we discuss different cellular pathways regulated by one of the first identified E3 ligase, NEDD4, focusing on its pathophysiological role, its known targets and modulators. In addition, we highlight small molecule inhibitors that act on NEDD4 and discuss new strategies to effectively target this E3 enzyme.
    MeSH term(s) Endosomal Sorting Complexes Required for Transport/metabolism ; Nedd4 Ubiquitin Protein Ligases/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
    Chemical Substances Endosomal Sorting Complexes Required for Transport ; Ubiquitin ; Nedd4 Ubiquitin Protein Ligases (EC 2.3.2.26) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2021-11-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20210731
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Correction: Role of the early secretory pathway in SARS-CoV-2 infection.

    Sicari, Daria / Chatziioannou, Aristotelis / Koutsandreas, Theodoros / Sitia, Roberto / Chevet, Eric

    The Journal of cell biology

    2020  Volume 219, Issue 9

    Keywords covid19
    Language English
    Publishing date 2020-08-25
    Publishing country United States
    Document type Journal Article ; Published Erratum
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.20200600508132020c
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Control of Protein Homeostasis in the Early Secretory Pathway: Current Status and Challenges.

    Sicari, Daria / Igbaria, Aeid / Chevet, Eric

    Cells

    2019  Volume 8, Issue 11

    Abstract: ...

    Abstract :
    MeSH term(s) Animals ; Endoplasmic Reticulum/metabolism ; Eukaryotic Cells/metabolism ; Golgi Apparatus/metabolism ; Homeostasis ; Humans ; Protein Biosynthesis/physiology ; Protein Folding ; Proteins/chemistry ; Proteins/metabolism ; Proteostasis/physiology ; Secretory Pathway/physiology
    Chemical Substances Proteins
    Language English
    Publishing date 2019-10-29
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells8111347
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  4. Article ; Online: Role of the early secretory pathway in SARS-CoV-2 infection.

    Sicari, Daria / Chatziioannou, Aristotelis / Koutsandreas, Theodoros / Sitia, Roberto / Chevet, Eric

    The Journal of cell biology

    2020  Volume 219, Issue 9

    Abstract: Similar to other RNA viruses, SARS-CoV-2 must (1) enter a target/host cell, (2) reprogram it to ensure its replication, (3) exit the host cell, and (4) repeat this cycle for exponential growth. During the exit step, the virus hijacks the sophisticated ... ...

    Abstract Similar to other RNA viruses, SARS-CoV-2 must (1) enter a target/host cell, (2) reprogram it to ensure its replication, (3) exit the host cell, and (4) repeat this cycle for exponential growth. During the exit step, the virus hijacks the sophisticated machineries that host cells employ to correctly fold, assemble, and transport proteins along the exocytic pathway. Therefore, secretory pathway-mediated assemblage and excretion of infective particles represent appealing targets to reduce the efficacy of virus biogenesis, if not to block it completely. Here, we analyze and discuss the contribution of the molecular machines operating in the early secretory pathway in the biogenesis of SARS-CoV-2 and their relevance for potential antiviral targeting. The fact that these molecular machines are conserved throughout evolution, together with the redundancy and tissue specificity of their components, provides opportunities in the search for unique proteins essential for SARS-CoV-2 biology that could also be targeted with therapeutic objectives. Finally, we provide an overview of recent evidence implicating proteins of the early secretory pathway as potential antiviral targets with effective therapeutic applications.
    MeSH term(s) Antiviral Agents/therapeutic use ; Betacoronavirus/drug effects ; Betacoronavirus/pathogenicity ; COVID-19 ; Coronavirus Infections/drug therapy ; Coronavirus Infections/virology ; Humans ; Pandemics ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/virology ; SARS-CoV-2 ; Secretory Pathway/drug effects ; Secretory Pathway/physiology ; Virus Replication/drug effects ; Virus Replication/physiology
    Chemical Substances Antiviral Agents
    Keywords covid19
    Language English
    Publishing date 2020-07-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202006005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.190: Show issues Location:
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  5. Article ; Online: Control of Protein Homeostasis in the Early Secretory Pathway

    Daria Sicari / Aeid Igbaria / Eric Chevet

    Cells, Vol 8, Iss 11, p

    Current Status and Challenges

    2019  Volume 1347

    Abstract: Discrimination between properly folded proteins and those that do not reach this state is necessary for cells to achieve functionality. Eukaryotic cells have evolved several mechanisms to ensure secretory protein quality control, which allows ... ...

    Abstract : Discrimination between properly folded proteins and those that do not reach this state is necessary for cells to achieve functionality. Eukaryotic cells have evolved several mechanisms to ensure secretory protein quality control, which allows efficiency and fidelity in protein production. Among the actors involved in such process, both endoplasmic reticulum (ER) and the Golgi complex play prominent roles in protein synthesis, biogenesis and secretion. ER and Golgi functions ensure that only properly folded proteins are allowed to flow through the secretory pathway while improperly folded proteins have to be eliminated to not impinge on cellular functions. Thus, complex quality control and degradation machineries are crucial to prevent the toxic accumulation of improperly folded proteins. However, in some instances, improperly folded proteins can escape the quality control systems thereby contributing to several human diseases. Herein, we summarize how the early secretory pathways copes with the accumulation of improperly folded proteins, and how insufficient handling can cause the development of several human diseases. Finally, we detail the genetic and pharmacologic approaches that could be used as potential therapeutic tools to treat these diseases.
    Keywords er stress ; golgi stress ; erad ; egad ; protein quality control ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2019-10-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article: Correction: Role of the early secretory pathway in SARS-CoV-2 infection

    Sicari, Daria / Chatziioannou, Aristotelis / Koutsandreas, Theodoros / Sitia, Roberto / Chevet, Eric

    J. cell. biol

    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #887245
    Database COVID19

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  7. Article ; Online: Correction

    Sicari, Daria / Chatziioannou, Aristotelis / Koutsandreas, Theodoros / Sitia, Roberto / Chevet, Eric

    Journal of Cell Biology

    Role of the early secretory pathway in SARS-CoV-2 infection

    2020  Volume 219, Issue 9

    Keywords Cell Biology ; covid19
    Language English
    Publisher Rockefeller University Press
    Publishing country us
    Document type Article ; Online
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.20200600508132020c
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Ub I Zs.190: Show issues Location:
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  8. Article: A guide to assessing endoplasmic reticulum homeostasis and stress in mammalian systems

    Sicari, Daria / Delaunay‐Moisan, Agnès / Combettes, Laurent / Chevet, Eric / Igbaria, Aeid

    FEBS journal. 2020 Jan., v. 287, no. 1

    2020  

    Abstract: The endoplasmic reticulum (ER) is a multifunctional organelle that constitutes the entry into the secretory pathway. The ER contributes to the maintenance of cellular calcium homeostasis, lipid synthesis and productive secretory, and transmembrane ... ...

    Abstract The endoplasmic reticulum (ER) is a multifunctional organelle that constitutes the entry into the secretory pathway. The ER contributes to the maintenance of cellular calcium homeostasis, lipid synthesis and productive secretory, and transmembrane protein folding. Physiological, chemical, and pathological factors that compromise ER homeostasis lead to endoplasmic reticulum stress (ER stress). To cope with this situation, cells activate an adaptive signaling pathway termed the unfolded protein response (UPR) that aims at restoring ER homeostasis. The UPR is transduced through post‐translational, translational, post‐transcriptional, and transcriptional mechanisms initiated by three ER‐resident sensors, inositol‐requiring protein 1α, activating transcription factor 6α, and PRKR‐like endoplasmic reticulum kinase. Determining the in and out of ER homeostasis control and UPR activation still represents a challenge for the community. Hence, standardized criteria and methodologies need to be proposed for monitoring ER homeostasis and ER stress in different model systems. Here, we summarize the pathways that are activated during ER stress and provide approaches aimed at assess ER homeostasis and stress in vitro and in vivo mammalian systems that can be used by researchers to plan and interpret experiments. We recommend the use of multiple assays to verify ER stress because no individual assay is guaranteed to be the most appropriate one.
    Keywords calcium ; endoplasmic reticulum ; endoplasmic reticulum stress ; homeostasis ; lipids ; mammals ; transcription (genetics) ; transcription factors ; transmembrane proteins ; unfolded protein response
    Language English
    Dates of publication 2020-01
    Size p. 27-42.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note NAL-AP-2-clean ; REVIEW
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.15107
    Database NAL-Catalogue (AGRICOLA)

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  9. Article ; Online: A virtuous cycle operated by ERp44 and ERGIC-53 guarantees proteostasis in the early secretory compartment.

    Tempio, Tiziana / Orsi, Andrea / Sicari, Daria / Valetti, Caterina / Yoboue, Edgar Djaha / Anelli, Tiziana / Sitia, Roberto

    iScience

    2021  Volume 24, Issue 3, Page(s) 102244

    Abstract: The composition of the secretome depends on the combined action of cargo receptors that facilitate protein transport and sequential checkpoints that restrict it to native conformers. Acting after endoplasmic reticulum (ER)-resident chaperones, ERp44 ... ...

    Abstract The composition of the secretome depends on the combined action of cargo receptors that facilitate protein transport and sequential checkpoints that restrict it to native conformers. Acting after endoplasmic reticulum (ER)-resident chaperones, ERp44 retrieves its clients from downstream compartments. To guarantee efficient quality control, ERp44 should exit the ER as rapidly as its clients, or more. Here, we show that appending ERp44 to different cargo proteins increases their secretion rates. ERp44 binds the cargo receptor ER-Golgi intermediate compartment (ERGIC)-53 in the ER to negotiate preferential loading into COPII vesicles. Silencing ERGIC-53, or competing for its COPII binding with 4-phenylbutyrate, causes secretion of Prdx4, an enzyme that relies on ERp44 for intracellular localization. In more acidic, zinc-rich downstream compartments, ERGIC-53 releases its clients and ERp44, which can bind and retrieve non-native conformers via KDEL receptors. By coupling the transport of cargoes and inspector proteins, cells ensure efficiency and fidelity of secretion.
    Language English
    Publishing date 2021-03-01
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2021.102244
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Role of the early secretory pathway in SARS-CoV-2 infection

    Sicari, Daria / Chatziioannou, Aristotelis / Koutsandreas, Theodoros / Sitia, Roberto / Chevet, Eric

    J. cell. biol

    Abstract: Similar to other RNA viruses, SARS-CoV-2 must (1) enter a target/host cell, (2) reprogram it to ensure its replication, (3) exit the host cell, and (4) repeat this cycle for exponential growth. During the exit step, the virus hijacks the sophisticated ... ...

    Abstract Similar to other RNA viruses, SARS-CoV-2 must (1) enter a target/host cell, (2) reprogram it to ensure its replication, (3) exit the host cell, and (4) repeat this cycle for exponential growth. During the exit step, the virus hijacks the sophisticated machineries that host cells employ to correctly fold, assemble, and transport proteins along the exocytic pathway. Therefore, secretory pathway-mediated assemblage and excretion of infective particles represent appealing targets to reduce the efficacy of virus biogenesis, if not to block it completely. Here, we analyze and discuss the contribution of the molecular machines operating in the early secretory pathway in the biogenesis of SARS-CoV-2 and their relevance for potential antiviral targeting. The fact that these molecular machines are conserved throughout evolution, together with the redundancy and tissue specificity of their components, provides opportunities in the search for unique proteins essential for SARS-CoV-2 biology that could also be targeted with therapeutic objectives. Finally, we provide an overview of recent evidence implicating proteins of the early secretory pathway as potential antiviral targets with effective therapeutic applications.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #691118
    Database COVID19

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