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  1. Article ; Online: Lysosomes as coordinators of cellular catabolism, metabolic signalling and organ physiology.

    Settembre, Carmine / Perera, Rushika M

    Nature reviews. Molecular cell biology

    2023  Volume 25, Issue 3, Page(s) 223–245

    Abstract: Every cell must satisfy basic requirements for nutrient sensing, utilization and recycling through macromolecular breakdown to coordinate programmes for growth, repair and stress adaptation. The lysosome orchestrates these key functions through the ... ...

    Abstract Every cell must satisfy basic requirements for nutrient sensing, utilization and recycling through macromolecular breakdown to coordinate programmes for growth, repair and stress adaptation. The lysosome orchestrates these key functions through the synchronised interplay between hydrolytic enzymes, nutrient transporters and signalling factors, which together enable metabolic coordination with other organelles and regulation of specific gene expression programmes. In this Review, we discuss recent findings on lysosome-dependent signalling pathways, focusing on how the lysosome senses nutrient availability through its physical and functional association with mechanistic target of rapamycin complex 1 (mTORC1) and how, in response, the microphthalmia/transcription factor E (MiT/TFE) transcription factors exert feedback regulation on lysosome biogenesis. We also highlight the emerging interactions of lysosomes with other organelles, which contribute to cellular homeostasis. Lastly, we discuss how lysosome dysfunction contributes to diverse disease pathologies and how inherited mutations that compromise lysosomal hydrolysis, transport or signalling components lead to multi-organ disorders with severe metabolic and neurological impact. A deeper comprehension of lysosomal composition and function, at both the cellular and organismal level, may uncover fundamental insights into human physiology and disease.
    MeSH term(s) Humans ; Signal Transduction/physiology ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Lysosomes/metabolism ; Homeostasis/physiology ; Autophagy/physiology
    Chemical Substances Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
    Language English
    Publishing date 2023-11-24
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-023-00676-x
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    Zs.A 5446: Show issues Location:
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  2. Article ; Online: Regulatory events controlling ER-phagy.

    Iavarone, Francescopaolo / Di Lorenzo, Giorgia / Settembre, Carmine

    Current opinion in cell biology

    2022  Volume 76, Page(s) 102084

    Abstract: Autophagy of the endoplasmic reticulum (ER), known as ER-phagy, is responsible for the degradation of ER portions by lysosomes. ER-phagy is induced in both physiological and stress conditions to maintain ER homeostasis and protein quality control. ER- ... ...

    Abstract Autophagy of the endoplasmic reticulum (ER), known as ER-phagy, is responsible for the degradation of ER portions by lysosomes. ER-phagy is induced in both physiological and stress conditions to maintain ER homeostasis and protein quality control. ER-phagy receptors and their interactors are key regulators of this process. Transcriptional and post-translational regulation of ER-phagy receptors have emerged as critical mechanisms for the modulation of ER-phagy, providing the first hints to understand how this process responds to the cellular needs. Here, we concisely review the main mechanisms regulating ER-phagy receptors and discuss their potential implications in diseases.
    MeSH term(s) Autophagy/physiology ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress/physiology ; Lysosomes/metabolism ; Membrane Proteins/metabolism
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2022-05-06
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2022.102084
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  3. Article ; Online: Beating the ER: novel insights into FAM134B function and regulation.

    De Leonibus, Chiara / Cinque, Laura / Settembre, Carmine

    The EMBO journal

    2020  Volume 39, Issue 5, Page(s) e104546

    Abstract: To maintain cellular homeostasis, the endoplasmic reticulum (ER) necessitates a continuous removal of ER fragments via a selective, receptor-mediated, form of autophagy known as ER-phagy. In this issue of The EMBO Journal, Jiang et al (2020) shed light ... ...

    Abstract To maintain cellular homeostasis, the endoplasmic reticulum (ER) necessitates a continuous removal of ER fragments via a selective, receptor-mediated, form of autophagy known as ER-phagy. In this issue of The EMBO Journal, Jiang et al (2020) shed light on how the best characterized autophagy receptor FAM134B mediates ER membrane fragmentation, the earliest event during ER-phagy. They propose a dynamic model for FAM134B protein oligomerization and ER membrane scission, which are driven by CAMK2B-mediated phosphorylation of the receptor and are altered in sensory neuropathy.
    MeSH term(s) Autophagy ; Carrier Proteins ; Endoplasmic Reticulum ; Homeostasis ; Membrane Proteins
    Chemical Substances Carrier Proteins ; Membrane Proteins
    Language English
    Publishing date 2020-02-19
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2020104546
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  4. Article: A mutation in the ZNF687 gene that is responsible for the severe form of Paget's disease of bone causes severely altered bone remodeling and promotes hepatocellular carcinoma onset in a knock-in mouse model.

    Russo, Sharon / Scotto di Carlo, Federica / Maurizi, Antonio / Fortunato, Giorgio / Teti, Anna / Licastro, Danilo / Settembre, Carmine / Mello, Tommaso / Gianfrancesco, Fernando

    Bone research

    2023  Volume 11, Issue 1, Page(s) 16

    Abstract: Paget's disease (PDB) is a late-onset bone remodeling disorder with a broad spectrum of symptoms and complications. One of the most aggressive forms is caused by the P937R mutation in the ZNF687 gene. Although the genetic involvement of ZNF687 in PDB has ...

    Abstract Paget's disease (PDB) is a late-onset bone remodeling disorder with a broad spectrum of symptoms and complications. One of the most aggressive forms is caused by the P937R mutation in the ZNF687 gene. Although the genetic involvement of ZNF687 in PDB has been extensively studied, the molecular mechanisms underlying this association remain unclear. Here, we describe the first Zfp687 knock-in mouse model and demonstrate that the mutation recapitulates the PDB phenotype, resulting in severely altered bone remodeling. Through microcomputed tomography analysis, we observed that 8-month-old mutant mice showed a mainly osteolytic phase, with a significant decrease in the trabecular bone volume affecting the femurs and the vertebrae. Conversely, osteoblast activity was deregulated, producing disorganized bone. Notably, this phenotype became pervasive in 16-month-old mice, where osteoblast function overtook bone resorption, as highlighted by the presence of woven bone in histological analyses, consistent with the PDB phenotype. Furthermore, we detected osteophytes and intervertebral disc degeneration, outlining for the first time the link between osteoarthritis and PDB in a PDB mouse model. RNA sequencing of wild-type and Zfp687 knockout RAW264.7 cells identified a set of genes involved in osteoclastogenesis potentially regulated by Zfp687, e.g., Tspan7, Cpe, Vegfc, and Ggt1, confirming its role in this process. Strikingly, in this mouse model, the mutation was also associated with a high penetrance of hepatocellular carcinomas. Thus, this study established an essential role of Zfp687 in the regulation of bone remodeling, offering the potential to therapeutically treat PDB, and underlines the oncogenic potential of ZNF687.
    Language English
    Publishing date 2023-03-14
    Publishing country China
    Document type Journal Article
    ZDB-ID 2803313-9
    ISSN 2095-6231 ; 2095-4700
    ISSN (online) 2095-6231
    ISSN 2095-4700
    DOI 10.1038/s41413-023-00250-3
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  5. Article: Transcriptional Regulation of Autophagy: Mechanisms and Diseases.

    Di Malta, Chiara / Cinque, Laura / Settembre, Carmine

    Frontiers in cell and developmental biology

    2019  Volume 7, Page(s) 114

    Abstract: Macro (Autophagy) is a catabolic process that relies on the cooperative function of two organelles: the lysosome and the autophagosome. The recent discovery of a transcriptional gene network that co-regulates the biogenesis and function of these two ... ...

    Abstract Macro (Autophagy) is a catabolic process that relies on the cooperative function of two organelles: the lysosome and the autophagosome. The recent discovery of a transcriptional gene network that co-regulates the biogenesis and function of these two organelles, and the identification of transcription factors, miRNAs and epigenetic regulators of autophagy, demonstrated that this catabolic process is controlled by both transcriptional and post-transcriptional mechanisms. In this review article, we discuss the nuclear events that control autophagy, focusing particularly on the role of the MiT/TFE transcription factor family. In addition, we will discuss evidence suggesting that the transcriptional regulation of autophagy could be targeted for the treatment of human genetic diseases, such as lysosomal storage disorders (LSDs) and neurodegeneration.
    Language English
    Publishing date 2019-07-02
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2019.00114
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  6. Article ; Online: Emerging lysosomal pathways for quality control at the endoplasmic reticulum.

    De Leonibus, Chiara / Cinque, Laura / Settembre, Carmine

    FEBS letters

    2019  Volume 593, Issue 17, Page(s) 2319–2329

    Abstract: Protein misfolding occurring in the endoplasmic reticulum (ER) might eventually lead to aggregation and cellular distress, and is a primary pathogenic mechanism in multiple human disorders. Mammals have developed evolutionary-conserved quality control ... ...

    Abstract Protein misfolding occurring in the endoplasmic reticulum (ER) might eventually lead to aggregation and cellular distress, and is a primary pathogenic mechanism in multiple human disorders. Mammals have developed evolutionary-conserved quality control mechanisms at the level of the ER. The best characterized is the ER-associated degradation (ERAD) pathway, through which misfolded proteins translocate from the ER to the cytosol and are subsequently proteasomally degraded. However, increasing evidence indicates that additional quality control mechanisms apply for misfolded ER clients that are not eligible for ERAD. This review focuses on the alternative, ERAD-independent, mechanisms of clearance of misfolded polypeptides from the ER. These processes, collectively referred to as ER-to-lysosome-associated degradation, involve ER-phagy, microautophagy or vesicular transport. The identification of the underlying molecular mechanisms is particularly important for developing new therapeutic approaches for human diseases associated with protein aggregate formation.
    MeSH term(s) Animals ; Autophagy ; Disease ; Endoplasmic Reticulum/metabolism ; Humans ; Lysosomes/metabolism
    Language English
    Publishing date 2019-08-13
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.13571
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    Zs.B 282: Show issues Location:
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  7. Article ; Online: MAPK15 protects from oxidative stress-dependent cellular senescence by inducing the mitophagic process.

    Franci, Lorenzo / Tubita, Alessandro / Bertolino, Franca Maria / Palma, Alessandro / Cannino, Giuseppe / Settembre, Carmine / Rasola, Andrea / Rovida, Elisabetta / Chiariello, Mario

    Aging cell

    2022  Volume 21, Issue 7, Page(s) e13620

    Abstract: Mitochondria are the major source of reactive oxygen species (ROS), whose aberrant production by dysfunctional mitochondria leads to oxidative stress, thus contributing to aging as well as neurodegenerative disorders and cancer. Cells efficiently ... ...

    Abstract Mitochondria are the major source of reactive oxygen species (ROS), whose aberrant production by dysfunctional mitochondria leads to oxidative stress, thus contributing to aging as well as neurodegenerative disorders and cancer. Cells efficiently eliminate damaged mitochondria through a selective type of autophagy, named mitophagy. Here, we demonstrate the involvement of the atypical MAP kinase family member MAPK15 in cellular senescence, by preserving mitochondrial quality, thanks to its ability to control mitophagy and, therefore, prevent oxidative stress. We indeed demonstrate that reduced MAPK15 expression strongly decreases mitochondrial respiration and ATP production, while increasing mitochondrial ROS levels. We show that MAPK15 controls the mitophagic process by stimulating ULK1-dependent PRKN Ser
    MeSH term(s) Autophagy/genetics ; Cellular Senescence/genetics ; Cellular Senescence/physiology ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; Mitophagy/genetics ; Mitophagy/physiology ; Oxidative Stress/genetics ; Oxidative Stress/physiology ; Reactive Oxygen Species/metabolism
    Chemical Substances Reactive Oxygen Species ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; MAPK15 protein, human (EC 2.7.11.24)
    Language English
    Publishing date 2022-06-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2113083-8
    ISSN 1474-9726 ; 1474-9718
    ISSN (online) 1474-9726
    ISSN 1474-9718
    DOI 10.1111/acel.13620
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    Zs.A 6581: Show issues Location:
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  8. Article ; Online: Transcriptional Regulation of Autophagy

    Chiara Di Malta / Laura Cinque / Carmine Settembre

    Frontiers in Cell and Developmental Biology, Vol

    Mechanisms and Diseases

    2019  Volume 7

    Abstract: Macro (Autophagy) is a catabolic process that relies on the cooperative function of two organelles: the lysosome and the autophagosome. The recent discovery of a transcriptional gene network that co-regulates the biogenesis and function of these two ... ...

    Abstract Macro (Autophagy) is a catabolic process that relies on the cooperative function of two organelles: the lysosome and the autophagosome. The recent discovery of a transcriptional gene network that co-regulates the biogenesis and function of these two organelles, and the identification of transcription factors, miRNAs and epigenetic regulators of autophagy, demonstrated that this catabolic process is controlled by both transcriptional and post-transcriptional mechanisms. In this review article, we discuss the nuclear events that control autophagy, focusing particularly on the role of the MiT/TFE transcription factor family. In addition, we will discuss evidence suggesting that the transcriptional regulation of autophagy could be targeted for the treatment of human genetic diseases, such as lysosomal storage disorders (LSDs) and neurodegeneration.
    Keywords autophagy ; TFEB ; genetic diseases ; nucleus ; transcription ; lysosomal storage disease ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2019-07-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Autophagy gets to the bone.

    Cinque, Laura / Forrester, Alison / Settembre, Carmine

    Cell cycle (Georgetown, Tex.)

    2016  Volume 15, Issue 7, Page(s) 871–872

    MeSH term(s) Autophagy ; Bone and Bones ; Cartilage ; Chondrocytes ; Collagen ; Humans
    Chemical Substances Collagen (9007-34-5)
    Language English
    Publishing date 2016-03-03
    Publishing country United States
    Document type Editorial ; Comment
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.1080/15384101.2016.1151724
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    Zs.A 5881: Show issues Location:
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  10. Article ; Online: New targets for old diseases: lessons from mucolipidosis type II.

    Settembre, Carmine / Ballabio, Andrea

    EMBO molecular medicine

    2013  Volume 5, Issue 12, Page(s) 1801–1803

    MeSH term(s) Animals ; Bone Development ; Female ; Humans ; Mucolipidoses/pathology ; Osteoclasts/metabolism
    Language English
    Publishing date 2013-11-08
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2467145-9
    ISSN 1757-4684 ; 1757-4676
    ISSN (online) 1757-4684
    ISSN 1757-4676
    DOI 10.1002/emmm.201303496
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