LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Back to previous search Search history
Advanced search

Your last searches

  1. AU="Mastrodonato, Valeria"
  2. AU="Ocak, Süheyla"
  3. AU="Bain, Joseph"
  4. AU="Müller, Alina"
  5. AU="Moreno, Jessica L"
  6. AU="Guimaraes-Ferreira, Lucas"
  7. AU="Bhandari, Ruchi"
  8. AU="Fichtner, Maximilian"
  9. AU="Dina, Yemisi"

Search results

Result 1 - 5 of total 5

Search options

  1. Article ; Online: How to use a multipurpose SNARE: The emerging role of Snap29 in cellular health.

    Mastrodonato, Valeria / Morelli, Elena / Vaccari, Thomas

    Cell stress

    2018  Volume 2, Issue 4, Page(s) 72–81

    Abstract: Despite extensive study, regulation of membrane trafficking is incompletely understood. In particular, the specific role of SNARE (Soluble NSF Attachment REceptor) proteins for distinct trafficking steps and their mechanism of action, beyond the core ... ...

    Abstract Despite extensive study, regulation of membrane trafficking is incompletely understood. In particular, the specific role of SNARE (Soluble NSF Attachment REceptor) proteins for distinct trafficking steps and their mechanism of action, beyond the core function in membrane fusion, are still elusive. Snap29 is a SNARE protein related to Snap25 that gathered a lot of attention in recent years. Here, we review the study of Snap29 and its emerging involvement in autophagy, a self eating process that is key to cell adaptation to changing environments, and in other trafficking pathways. We also discuss Snap29 role in synaptic transmission and in cell division, which might extend the repertoire of SNARE-mediated functions. Finally, we present evidence connecting Snap29 to human disease, highlighting the importance of Snap29 function in tissue development and homeostasis.
    Language English
    Publishing date 2018-03-22
    Publishing country Austria
    Document type Journal Article ; Review
    ISSN 2523-0204
    ISSN (online) 2523-0204
    DOI 10.15698/cst2018.04.130
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: A genetic model of CEDNIK syndrome in zebrafish highlights the role of the SNARE protein Snap29 in neuromotor and epidermal development.

    Mastrodonato, Valeria / Beznoussenko, Galina / Mironov, Alexandre / Ferrari, Laura / Deflorian, Gianluca / Vaccari, Thomas

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 1211

    Abstract: Homozygous mutations in SNAP29, encoding a SNARE protein mainly involved in membrane fusion, cause CEDNIK (Cerebral Dysgenesis, Neuropathy, Ichthyosis and Keratoderma), a rare congenital neurocutaneous syndrome associated with short life expectancy, ... ...

    Abstract Homozygous mutations in SNAP29, encoding a SNARE protein mainly involved in membrane fusion, cause CEDNIK (Cerebral Dysgenesis, Neuropathy, Ichthyosis and Keratoderma), a rare congenital neurocutaneous syndrome associated with short life expectancy, whose pathogenesis is unclear. Here, we report the analysis of the first genetic model of CEDNIK in zebrafish. Strikingly, homozygous snap29 mutant larvae display CEDNIK-like features, such as microcephaly and skin defects. Consistent with Snap29 role in membrane fusion during autophagy, we observe accumulation of the autophagy markers p62 and LC3, and formation of aberrant multilamellar organelles and mitochondria. Importantly, we find high levels of apoptotic cell death during early development that might play a yet uncharacterized role in CEDNIK pathogenesis. Mutant larvae also display mouth opening problems, feeding impairment and swimming difficulties. These alterations correlate with defective trigeminal nerve formation and excess axonal branching. Since the paralog Snap25 is known to promote axonal branching, Snap29 might act in opposition with, or modulate Snap25 activity during neurodevelopment. Our vertebrate genetic model of CEDNIK extends the description in vivo of the multisystem defects due to loss of Snap29 and could provide the base to test compounds that might ameliorate traits of the disease.
    MeSH term(s) Animals ; Autophagy ; Humans ; Keratoderma, Palmoplantar/genetics ; Keratoderma, Palmoplantar/metabolism ; Keratoderma, Palmoplantar/physiopathology ; Membrane Fusion ; Models, Genetic ; Mutation ; Nervous System Malformations/metabolism ; Neurocutaneous Syndromes/genetics ; Neurocutaneous Syndromes/metabolism ; Neurocutaneous Syndromes/physiopathology ; Phenotype ; Protein Binding ; Qb-SNARE Proteins/metabolism ; Qc-SNARE Proteins/metabolism ; SNARE Proteins/metabolism ; SNARE Proteins/physiology ; Synaptosomal-Associated Protein 25/metabolism ; Synaptosomal-Associated Protein 25/physiology ; Zebrafish/metabolism ; Zebrafish Proteins/metabolism ; Zebrafish Proteins/physiology
    Chemical Substances Qb-SNARE Proteins ; Qc-SNARE Proteins ; SNAP29 protein, human ; SNARE Proteins ; Snap29 protein, zebrafish ; Synaptosomal-Associated Protein 25 ; Zebrafish Proteins
    Language English
    Publishing date 2019-02-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-018-37780-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: ESCRT genes and regulation of developmental signaling.

    Horner, David S / Pasini, Maria E / Beltrame, Monica / Mastrodonato, Valeria / Morelli, Elena / Vaccari, Thomas

    Seminars in cell & developmental biology

    2017  Volume 74, Page(s) 29–39

    Abstract: ESCRT (Endosomal Sorting Complex Required for Transport) proteins have been shown to control an increasing number of membrane-associated processes. Some of these, and prominently regulation of receptor trafficking, profoundly shape signal transduction. ... ...

    Abstract ESCRT (Endosomal Sorting Complex Required for Transport) proteins have been shown to control an increasing number of membrane-associated processes. Some of these, and prominently regulation of receptor trafficking, profoundly shape signal transduction. Evidence in fungi, plants and multiple animal models support the emerging concept that ESCRTs are main actors in coordination of signaling with the changes in cells and tissues occurring during development and homeostasis. Consistent with their pleiotropic function, ESCRTs are regulated in multiple ways to tailor signaling to developmental and homeostatic needs. ESCRT activity is crucial to correct execution of developmental programs, especially at key transitions, allowing eukaryotes to thrive and preventing appearance of congenital defects.
    MeSH term(s) Animals ; Biological Transport ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; Central Nervous System/metabolism ; Endosomal Sorting Complexes Required for Transport/genetics ; Endosomal Sorting Complexes Required for Transport/metabolism ; Endosomes/metabolism ; Humans ; Signal Transduction/genetics
    Chemical Substances Endosomal Sorting Complexes Required for Transport
    Language English
    Publishing date 2017-08-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2017.08.038
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2918: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: An essential step of kinetochore formation controlled by the SNARE protein Snap29.

    Morelli, Elena / Mastrodonato, Valeria / Beznoussenko, Galina V / Mironov, Alexandre A / Tognon, Emiliana / Vaccari, Thomas

    The EMBO journal

    2016  Volume 35, Issue 20, Page(s) 2223–2237

    Abstract: The kinetochore is an essential structure that mediates accurate chromosome segregation in mitosis and meiosis. While many of the kinetochore components have been identified, the mechanisms of kinetochore assembly remain elusive. Here, we identify a ... ...

    Abstract The kinetochore is an essential structure that mediates accurate chromosome segregation in mitosis and meiosis. While many of the kinetochore components have been identified, the mechanisms of kinetochore assembly remain elusive. Here, we identify a novel role for Snap29, an unconventional SNARE, in promoting kinetochore assembly during mitosis in Drosophila and human cells. Snap29 localizes to the outer kinetochore and prevents chromosome mis-segregation and the formation of cells with fragmented nuclei. Snap29 promotes accurate chromosome segregation by mediating the recruitment of Knl1 at the kinetochore and ensuring stable microtubule attachments. Correct Knl1 localization to kinetochore requires human or Drosophila Snap29, and is prevented by a Snap29 point mutant that blocks Snap29 release from SNARE fusion complexes. Such mutant causes ectopic Knl1 recruitment to trafficking compartments. We propose that part of the outer kinetochore is functionally similar to membrane fusion interfaces.
    MeSH term(s) Animals ; Cell Line ; Drosophila ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; HeLa Cells ; Humans ; Kinetochores/metabolism ; Microtubule-Associated Proteins/metabolism ; Mitosis ; Qb-SNARE Proteins/genetics ; Qb-SNARE Proteins/metabolism ; Qc-SNARE Proteins/genetics ; Qc-SNARE Proteins/metabolism ; SNARE Proteins/genetics ; SNARE Proteins/metabolism
    Chemical Substances Drosophila Proteins ; Knl1 protein, human ; Microtubule-Associated Proteins ; Qb-SNARE Proteins ; Qc-SNARE Proteins ; SNAP29 protein, human ; SNARE Proteins ; Snap29 protein, Drosophila
    Language English
    Publishing date 2016-09-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.201693991
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 100: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: Multiple functions of the SNARE protein Snap29 in autophagy, endocytic, and exocytic trafficking during epithelial formation in Drosophila.

    Morelli, Elena / Ginefra, Pierpaolo / Mastrodonato, Valeria / Beznoussenko, Galina V / Rusten, Tor Erik / Bilder, David / Stenmark, Harald / Mironov, Alexandre A / Vaccari, Thomas

    Autophagy

    2014  Volume 10, Issue 12, Page(s) 2251–2268

    Abstract: How autophagic degradation is linked to endosomal trafficking routes is little known. Here we screened a collection of uncharacterized Drosophila mutants affecting membrane transport to identify new genes that also have a role in autophagy. We isolated a ...

    Abstract How autophagic degradation is linked to endosomal trafficking routes is little known. Here we screened a collection of uncharacterized Drosophila mutants affecting membrane transport to identify new genes that also have a role in autophagy. We isolated a loss of function mutant in Snap29 (Synaptosomal-associated protein 29 kDa), the gene encoding the Drosophila homolog of the human protein SNAP29 and have characterized its function in vivo. Snap29 contains 2 soluble NSF attachment protein receptor (SNARE) domains and a asparagine-proline-phenylalanine (NPF motif) at its N terminus and rescue experiments indicate that both SNARE domains are required for function, whereas the NPF motif is in part dispensable. We find that Snap29 interacts with SNARE proteins, localizes to multiple trafficking organelles, and is required for protein trafficking and for proper Golgi apparatus morphology. Developing tissue lacking Snap29 displays distinctive epithelial architecture defects and accumulates large amounts of autophagosomes, highlighting a major role of Snap29 in autophagy and secretion. Mutants for autophagy genes do not display epithelial architecture or secretion defects, suggesting that the these alterations of the Snap29 mutant are unlikely to be caused by the impairment of autophagy. In contrast, we find evidence of elevated levels of hop-Stat92E (hopscotch-signal transducer and activator of transcription protein at 92E) ligand, receptor, and associated signaling, which might underlie the epithelial defects. In summary, our findings support a role of Snap29 at key steps of membrane trafficking, and predict that signaling defects may contribute to the pathogenesis of cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma (CEDNIK), a human congenital syndrome due to loss of Snap29.
    MeSH term(s) Animals ; Autophagy/physiology ; Cell Movement/physiology ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Endosomes/metabolism ; Exosomes/metabolism ; Humans ; Phagosomes/metabolism ; Protein Binding/physiology ; Protein Transport/physiology ; Qb-SNARE Proteins/metabolism ; Qc-SNARE Proteins/metabolism ; SNARE Proteins/metabolism ; Vesicular Transport Proteins/metabolism
    Chemical Substances Drosophila Proteins ; Qb-SNARE Proteins ; Qc-SNARE Proteins ; SNAP29 protein, human ; SNARE Proteins ; Snap29 protein, Drosophila ; Vesicular Transport Proteins
    Language English
    Publishing date 2014-12-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/15548627.2014.981913
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6741: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top