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  1. Article ; Online: Proteolysis at work: when time matters for a sensory organelle.

    Senatore, Emanuela / Feliciello, Antonio

    BioEssays : news and reviews in molecular, cellular and developmental biology

    2022  Volume 44, Issue 9, Page(s) e2200137

    MeSH term(s) Organelles/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
    Chemical Substances Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2022-07-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 50140-2
    ISSN 1521-1878 ; 0265-9247
    ISSN (online) 1521-1878
    ISSN 0265-9247
    DOI 10.1002/bies.202200137
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2024: Show issues Location:
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  2. Article ; Online: Control of Mitochondrial Activity by the Ubiquitin Code in Health and Cancer.

    Rinaldi, Laura / Senatore, Emanuela / Iannucci, Rosa / Chiuso, Francesco / Feliciello, Antonio

    Cells

    2023  Volume 12, Issue 2

    Abstract: Cellular homeostasis is tightly connected to the broad variety of mitochondrial functions. To stay healthy, cells need a constant supply of nutrients, energy production and antioxidants defenses, undergoing programmed death when a serious, irreversible ... ...

    Abstract Cellular homeostasis is tightly connected to the broad variety of mitochondrial functions. To stay healthy, cells need a constant supply of nutrients, energy production and antioxidants defenses, undergoing programmed death when a serious, irreversible damage occurs. The key element of a functional integration of all these processes is the correct crosstalk between cell signaling and mitochondrial activities. Once this crosstalk is interrupted, the cell is not able to communicate its needs to mitochondria, resulting in oxidative stress and development of pathological conditions. Conversely, dysfunctional mitochondria may affect cell viability, even in the presence of nutrients supply and energy production, indicating the existence of feed-back control mechanisms between mitochondria and other cellular compartments. The ubiquitin proteasome system (UPS) is a multi-step biochemical pathway that, through the conjugation of ubiquitin moieties to specific protein substrates, controls cellular proteostasis and signaling, removing damaged or aged proteins that might otherwise accumulate and affect cell viability. In response to specific needs or changed extracellular microenvironment, the UPS modulates the turnover of mitochondrial proteins, thus influencing the organelle shape, dynamics and function. Alterations of the dynamic and reciprocal regulation between mitochondria and UPS underpin genetic and proliferative disorders. This review focuses on the mitochondrial metabolism and activities supervised by UPS and examines how deregulation of this control mechanism results in proliferative disorders and cancer.
    MeSH term(s) Humans ; Aged ; Ubiquitin/metabolism ; Mitochondria/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Signal Transduction ; Mitochondrial Proteins/metabolism ; Neoplasms/metabolism ; Tumor Microenvironment
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Mitochondrial Proteins
    Language English
    Publishing date 2023-01-05
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells12020234
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Experimental review of hypernuclear physics: recent achievements and future perspectives.

    Feliciello, A / Nagae, T

    Reports on progress in physics. Physical Society (Great Britain)

    2015  Volume 78, Issue 9, Page(s) 96301

    Abstract: Since the shutdown of several old proton synchrotrons, which played a fundamental role in the second generation experiments in hypernuclear physics performed in Europe, USA and Japan, some new experimental setups aiming to achieve sub-MeV energy ... ...

    Abstract Since the shutdown of several old proton synchrotrons, which played a fundamental role in the second generation experiments in hypernuclear physics performed in Europe, USA and Japan, some new experimental setups aiming to achieve sub-MeV energy resolution have been operating for a long time. Over the last decade the hypernuclear physics community has been committed to carrying out several third generation experiments by exploiting the potential offered by new accelerators, such as a continuous electron beam machine and a ϕ-factory. Large data samples were collected on specific items thanks to dedicated facilities and experimental apparatuses. The attention was mainly focused on both high-resolution spectroscopy and the decay mode study of single Λ-hypernuclei. Nowadays this phase is over but, until recently, important and, to some extent, unexpected results were achieved. An updated review of selected experimental results is presented, as well as a survey of perspectives for future studies.
    Language English
    Publishing date 2015-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 205657-4
    ISSN 1361-6633 ; 0034-4885
    ISSN (online) 1361-6633
    ISSN 0034-4885
    DOI 10.1088/0034-4885/78/9/096301
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Pathophysiology of Primary Cilia: Signaling and Proteostasis Regulation.

    Senatore, Emanuela / Iannucci, Rosa / Chiuso, Francesco / Delle Donne, Rossella / Rinaldi, Laura / Feliciello, Antonio

    Frontiers in cell and developmental biology

    2022  Volume 10, Page(s) 833086

    Abstract: Primary cilia are microtubule-based, non-motile sensory organelles present in most types of growth-arrested eukaryotic cells. They are transduction hubs that receive and transmit external signals to the cells in order to control growth, differentiation ... ...

    Abstract Primary cilia are microtubule-based, non-motile sensory organelles present in most types of growth-arrested eukaryotic cells. They are transduction hubs that receive and transmit external signals to the cells in order to control growth, differentiation and development. Mutations of genes involved in the formation, maintenance or disassembly of ciliary structures cause a wide array of developmental genetic disorders, also known as ciliopathies. The primary cilium is formed during G1 in the cell cycle and disassembles at the G2/M transition. Following the completion of the cell division, the cilium reassembles in G1. This cycle is finely regulated at multiple levels. The ubiquitin-proteasome system (UPS) and the autophagy machinery, two main protein degradative systems in cells, play a fundamental role in cilium dynamics. Evidence indicate that UPS, autophagy and signaling pathways may act in synergy to control the ciliary homeostasis. However, the mechanisms involved and the links between these regulatory systems and cilium biogenesis, dynamics and signaling are not well defined yet. Here, we discuss the reciprocal regulation of signaling pathways and proteolytic machineries in the control of the assembly and disassembly of the primary cilium, and the impact of the derangement of these regulatory networks in human ciliopathies.
    Language English
    Publishing date 2022-05-11
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2022.833086
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Metabolic rewiring and autophagy inhibition correct lysosomal storage disease in mucopolysaccharidosis IIIB.

    Scarcella, Melania / Scerra, Gianluca / Ciampa, Mariangela / Caterino, Marianna / Costanzo, Michele / Rinaldi, Laura / Feliciello, Antonio / Anzilotti, Serenella / Fiorentino, Chiara / Renna, Maurizio / Ruoppolo, Margherita / Pavone, Luigi Michele / D'Agostino, Massimo / De Pasquale, Valeria

    iScience

    2024  Volume 27, Issue 3, Page(s) 108959

    Abstract: Mucopolysaccharidoses (MPSs) are lysosomal disorders with neurological involvement for which no cure exists. Here, we show that recombinant NK1 fragment of hepatocyte growth factor rescues substrate accumulation and lysosomal defects in MPS I, IIIA and ... ...

    Abstract Mucopolysaccharidoses (MPSs) are lysosomal disorders with neurological involvement for which no cure exists. Here, we show that recombinant NK1 fragment of hepatocyte growth factor rescues substrate accumulation and lysosomal defects in MPS I, IIIA and IIIB patient fibroblasts. We investigated PI3K/Akt pathway, which is of crucial importance for neuronal function and survival, and demonstrate that PI3K inhibition abolishes NK1 therapeutic effects. We identified that autophagy inhibition, by Beclin1 silencing, reduces MPS IIIB phenotype and that NK1 downregulates autophagic-lysosome (ALP) gene expression, suggesting a possible contribution of autophagosome biogenesis in MPS. Indeed, metabolomic analyses revealed defects of mitochondrial activity accompanied by anaerobic metabolism and inhibition of AMP-activated protein kinase (AMPK), which acts on metabolism and autophagy, rescues lysosomal defects. These results provide insights into the molecular mechanisms of MPS IIIB physiopathology, supporting the development of new promising approaches based on autophagy inhibition and metabolic rewiring to correct lysosomal pathology in MPSs.
    Language English
    Publishing date 2024-01-29
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2024.108959
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  6. Article ; Online: Ubiquitylation of BBSome is required for ciliary assembly and signaling.

    Chiuso, Francesco / Delle Donne, Rossella / Giamundo, Giuliana / Rinaldi, Laura / Borzacchiello, Domenica / Moraca, Federica / Intartaglia, Daniela / Iannucci, Rosa / Senatore, Emanuela / Lignitto, Luca / Garbi, Corrado / Conflitti, Paolo / Catalanotti, Bruno / Conte, Ivan / Feliciello, Antonio

    EMBO reports

    2023  Volume 24, Issue 4, Page(s) e55571

    Abstract: Bardet-Biedl syndrome (BBS) is a ciliopathy characterized by retinal degeneration, obesity, renal abnormalities, postaxial polydactyly, and developmental defects. Genes mutated in BBS encode for components and regulators of the BBSome, an octameric ... ...

    Abstract Bardet-Biedl syndrome (BBS) is a ciliopathy characterized by retinal degeneration, obesity, renal abnormalities, postaxial polydactyly, and developmental defects. Genes mutated in BBS encode for components and regulators of the BBSome, an octameric complex that controls the trafficking of cargos and receptors within the primary cilium. Although both structure and function of the BBSome have been extensively studied, the impact of ubiquitin signaling on BBSome is largely unknown. We identify the E3 ubiquitin ligase PJA2 as a novel resident of the ciliary compartment and regulator of the BBSome. Upon GPCR-cAMP stimulation, PJA2 ubiquitylates BBSome subunits. We demonstrate that ubiquitylation of BBS1 at lysine 143 increases the stability of the BBSome and promotes its binding to BBS3, an Arf-like GTPase protein controlling the targeting of the BBSome to the ciliary membrane. Downregulation of PJA2 or expression of a ubiquitylation-defective BBS1 mutant (BBS1
    MeSH term(s) Animals ; Cilia/metabolism ; Protein Transport ; Signal Transduction ; Bardet-Biedl Syndrome/genetics ; Receptors, G-Protein-Coupled/genetics ; Ubiquitination
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2023-02-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.202255571
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5433: 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)
    Zs.MG 41: Show issues

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  7. Article: Mitochondrial Homeostasis and Signaling in Parkinson's Disease.

    Scorziello, Antonella / Borzacchiello, Domenica / Sisalli, Maria Jose / Di Martino, Rossana / Morelli, Micaela / Feliciello, Antonio

    Frontiers in aging neuroscience

    2020  Volume 12, Page(s) 100

    Abstract: The loss of dopaminergic (DA) neurons in ... ...

    Abstract The loss of dopaminergic (DA) neurons in the
    Language English
    Publishing date 2020-04-21
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2558898-9
    ISSN 1663-4365
    ISSN 1663-4365
    DOI 10.3389/fnagi.2020.00100
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  8. Article ; Online: Ncx3-Induced Mitochondrial Dysfunction in Midbrain Leads to Neuroinflammation in Striatum of A53t-α-Synuclein Transgenic Old Mice.

    Di Martino, Rossana / Sisalli, Maria Josè / Sirabella, Rossana / Della Notte, Salvatore / Borzacchiello, Domenica / Feliciello, Antonio / Annunziato, Lucio / Scorziello, Antonella

    International journal of molecular sciences

    2021  Volume 22, Issue 15

    Abstract: The exact mechanism underlying selective dopaminergic neurodegeneration is not completely understood. The complex interplay among toxic alpha-synuclein aggregates, oxidative stress, altered intracellular ... ...

    Abstract The exact mechanism underlying selective dopaminergic neurodegeneration is not completely understood. The complex interplay among toxic alpha-synuclein aggregates, oxidative stress, altered intracellular Ca
    MeSH term(s) Animals ; Astrocytes/metabolism ; Calcium/metabolism ; Cells, Cultured ; Dopaminergic Neurons/metabolism ; Mesencephalon/cytology ; Mesencephalon/metabolism ; Mice ; Mice, Inbred C57BL ; Mitochondria/metabolism ; Mutation, Missense ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Sodium-Calcium Exchanger/genetics ; Sodium-Calcium Exchanger/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
    Chemical Substances SLC38A3 protein, human ; Sodium-Calcium Exchanger ; alpha-Synuclein ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2021-07-30
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22158177
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  9. Article: Exploring the Leukemogenic Potential of GATA-1

    Trombetti, Silvia / Sessa, Raffaele / Catapano, Rosa / Rinaldi, Laura / Lo Bianco, Alessandra / Feliciello, Antonio / Izzo, Paola / Grosso, Michela

    Antioxidants (Basel, Switzerland)

    2021  Volume 10, Issue 10

    Abstract: GATA-1 is a key regulator of hematopoiesis. A balanced ratio of its two isoforms, GATA- ... ...

    Abstract GATA-1 is a key regulator of hematopoiesis. A balanced ratio of its two isoforms, GATA-1
    Language English
    Publishing date 2021-10-12
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox10101603
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  10. Article ; Online: Downregulation of praja2 restrains endocytosis and boosts tyrosine kinase receptors in kidney cancer.

    Rinaldi, Laura / Chiuso, Francesco / Senatore, Emanuela / Borzacchiello, Domenica / Lignitto, Luca / Iannucci, Rosa / Donne, Rossella Delle / Fuggi, Mariano / Reale, Carla / Russo, Filomena / Russo, Nicola Antonino / Giurato, Giorgio / Rizzo, Francesca / Sellitto, Assunta / Santangelo, Michele / De Biase, Davide / Paciello, Orlando / D'Ambrosio, Chiara / Amente, Stefano /
    Garbi, Corrado / Dalla, Emiliano / Scaloni, Andrea / Weisz, Alessandro / Ambrosino, Concetta / Insabato, Luigi / Feliciello, Antonio

    Communications biology

    2024  Volume 7, Issue 1, Page(s) 208

    Abstract: Clear cell renal cell carcinoma (ccRCC) is the most common kidney cancer in the adult population. Late diagnosis, resistance to therapeutics and recurrence of metastatic lesions account for the highest mortality rate among kidney cancer patients. ... ...

    Abstract Clear cell renal cell carcinoma (ccRCC) is the most common kidney cancer in the adult population. Late diagnosis, resistance to therapeutics and recurrence of metastatic lesions account for the highest mortality rate among kidney cancer patients. Identifying novel biomarkers for early cancer detection and elucidating the mechanisms underlying ccRCC will provide clues to treat this aggressive malignant tumor. Here, we report that the ubiquitin ligase praja2 forms a complex with-and ubiquitylates the AP2 adapter complex, contributing to receptor endocytosis and clearance. In human RCC tissues and cells, downregulation of praja2 by oncogenic miRNAs (oncomiRs) and the proteasome markedly impairs endocytosis and clearance of the epidermal growth factor receptor (EGFR), and amplifies downstream mitogenic and proliferative signaling. Restoring praja2 levels in RCC cells downregulates EGFR, rewires cancer cell metabolism and ultimately inhibits tumor cell growth and metastasis. Accordingly, genetic ablation of praja2 in mice upregulates RTKs (i.e. EGFR and VEGFR) and induces epithelial and vascular alterations in the kidney tissue.In summary, our findings identify a regulatory loop between oncomiRs and the ubiquitin proteasome system that finely controls RTKs endocytosis and clearance, positively impacting mitogenic signaling and kidney cancer growth.
    MeSH term(s) Adult ; Animals ; Humans ; Mice ; Carcinoma, Renal Cell/genetics ; Carcinoma, Renal Cell/pathology ; Down-Regulation ; Endocytosis ; ErbB Receptors/genetics ; ErbB Receptors/metabolism ; Kidney Neoplasms/genetics ; Kidney Neoplasms/pathology ; Proteasome Endopeptidase Complex/metabolism ; Receptor Protein-Tyrosine Kinases/genetics ; Ubiquitin/metabolism
    Chemical Substances ErbB Receptors (EC 2.7.10.1) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; Ubiquitin ; PJA2 protein, human (EC 2.3.2.27) ; PJA2 protein, mouse (EC 2.3.2.27)
    Language English
    Publishing date 2024-02-20
    Publishing country England
    Document type Journal Article
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-024-05823-4
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