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  1. Article ; Online: Generation of the short TRIM32 isoform is regulated by Lys 247 acetylation and a PEST sequence.

    Garcia-Garcia, Juncal / Overå, Katrine Stange / Khan, Waqas / Sjøttem, Eva

    PloS one

    2021  Volume 16, Issue 5, Page(s) e0251279

    Abstract: TRIM32 is an E3 ligase implicated in diverse biological pathways and pathologies such as muscular dystrophy and cancer. TRIM32 are expressed both as full-length proteins, and as a truncated protein. The mechanisms for regulating these isoforms are poorly ...

    Abstract TRIM32 is an E3 ligase implicated in diverse biological pathways and pathologies such as muscular dystrophy and cancer. TRIM32 are expressed both as full-length proteins, and as a truncated protein. The mechanisms for regulating these isoforms are poorly understood. Here we identify a PEST sequence in TRIM32 located in the unstructured region between the RING-BBox-CoiledCoil domains and the NHL repeats. The PEST sequence directs cleavage of TRIM32, generating a truncated protein similarly to the short isoform. We map three lysine residues that regulate PEST mediated cleavage and auto-ubiquitylation activity of TRIM32. Mimicking acetylation of lysine K247 completely inhibits TRIM32 cleavage, while the lysines K50 and K401 are implicated in auto-ubiquitylation activity. We show that the short isoform of TRIM32 is catalytic inactive, suggesting a dominant negative role. These findings uncover that TRIM32 is regulated by post-translational modifications of three lysine residues, and a conserved PEST sequence.
    MeSH term(s) Acetylation ; Cell Line ; HEK293 Cells ; Humans ; Lysine/genetics ; Muscular Dystrophies, Limb-Girdle/genetics ; Protein Binding/genetics ; Protein Isoforms/genetics ; Protein Processing, Post-Translational/genetics ; Transcription Factors/genetics ; Tripartite Motif Proteins/genetics ; Ubiquitin-Protein Ligases/genetics ; Ubiquitination/genetics
    Chemical Substances Protein Isoforms ; Transcription Factors ; Tripartite Motif Proteins ; TRIM32 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2021-05-17
    Publishing country United States
    Document type Journal Article
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0251279
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Wild Animals in Captivity: An Analysis of Parasite Biodiversity and Transmission among Animals at Two Zoological Institutions with Different Typologies.

    Esteban-Sánchez, Lorena / García-Rodríguez, Juan José / García-García, Juncal / Martínez-Nevado, Eva / de la Riva-Fraga, Manuel Antonio / Ponce-Gordo, Francisco

    Animals : an open access journal from MDPI

    2024  Volume 14, Issue 5

    Abstract: We have conducted a 10-year-long coprological study of the animals housed in two zoological institutions (ZooAquarium and Faunia, Madrid, Spain) to assess the parasite biodiversity, prevalence, and their relation with host class, diet, and enclosure type ...

    Abstract We have conducted a 10-year-long coprological study of the animals housed in two zoological institutions (ZooAquarium and Faunia, Madrid, Spain) to assess the parasite biodiversity, prevalence, and their relation with host class, diet, and enclosure type (soil type and level of isolation from wild fauna). A total of 4476 faecal samples from 132 mammal species and 951 samples from 86 avian species were examined. The results indicated that only 12.8% of avian species had parasites at least once during the study period, whereas 62.1% of mammal species tested positive. Predominantly, protists (
    Language English
    Publishing date 2024-03-06
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2606558-7
    ISSN 2076-2615
    ISSN 2076-2615
    DOI 10.3390/ani14050813
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: TRIM27 is an autophagy substrate facilitating mitochondria clustering and mitophagy via phosphorylated TBK1

    Garcia‐Garcia, Juncal / Berge, Anne Kristin McLaren / Overå, Katrine Stange / Larsen, Kenneth Bowitz / Bhujabal, Zambarlal / Brech, Andreas / Abudu, Yakubu Princely / Lamark, Trond / Johansen, Terje / Sjøttem, Eva

    The FEBS Journal. 2023 Feb., v. 290, no. 4 p.1096-1116

    2023  

    Abstract: Tripartite motif‐containing protein 27 (TRIM27/also called RFP) is a multifunctional ubiquitin E3 ligase involved in numerous cellular functions, such as proliferation, apoptosis, regulation of the NF‐kB pathway, endosomal recycling and the innate immune ...

    Abstract Tripartite motif‐containing protein 27 (TRIM27/also called RFP) is a multifunctional ubiquitin E3 ligase involved in numerous cellular functions, such as proliferation, apoptosis, regulation of the NF‐kB pathway, endosomal recycling and the innate immune response. TRIM27 interacts directly with TANK‐binding kinase 1 (TBK1) and regulates its stability. TBK1 in complex with autophagy receptors is recruited to ubiquitin chains assembled on the mitochondrial outer membrane promoting mitophagy. Here, we identify TRIM27 as an autophagy substrate, depending on ATG7, ATG9 and autophagy receptors for its lysosomal degradation. We show that TRIM27 forms ubiquitylated cytoplasmic bodies that co‐localize with autophagy receptors. Surprisingly, we observed that induced expression of EGFP‐TRIM27 in HEK293 FlpIn TRIM27 knockout cells mediates mitochondrial clustering. TRIM27 interacts with autophagy receptor SQSTM1/p62, and the TRIM27‐mediated mitochondrial clustering is facilitated by SQSTM/p62. We show that phosphorylated TBK1 is recruited to the clustered mitochondria. Moreover, induced mitophagy activity is reduced in HEK293 FlpIn TRIM27 knockout cells, while re‐introduction of EGFP‐TRIM27 completely restores the mitophagy activity. Inhibition of TBK1 reduces mitophagy in HEK293 FlpIn cells and in the reconstituted EGFP‐TRIM27‐expressing cells, but not in HEK293 FlpIn TRIM27 knockout cells. Altogether, these data reveal novel roles for TRIM27 in mitophagy, facilitating mitochondrial clustering via SQSTM1/p62 and mitophagy via stabilization of phosphorylated TBK1 on mitochondria.
    Keywords apoptosis ; innate immunity ; mitochondria ; mitophagy ; transcription factor NF-kappa B ; ubiquitin ; ubiquitin-protein ligase
    Language English
    Dates of publication 2023-02
    Size p. 1096-1116.
    Publishing place John Wiley & Sons, Ltd
    Document type Article ; Online
    Note JOURNAL ARTICLE
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.16628
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2006/704: Show issues

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  4. Article ; Online: TRIM27 is an autophagy substrate facilitating mitochondria clustering and mitophagy via phosphorylated TBK1.

    Garcia-Garcia, Juncal / Berge, Anne Kristin McLaren / Overå, Katrine Stange / Larsen, Kenneth Bowitz / Bhujabal, Zambarlal / Brech, Andreas / Abudu, Yakubu Princely / Lamark, Trond / Johansen, Terje / Sjøttem, Eva

    The FEBS journal

    2022  Volume 290, Issue 4, Page(s) 1096–1116

    Abstract: Tripartite motif-containing protein 27 (TRIM27/also called RFP) is a multifunctional ubiquitin E3 ligase involved in numerous cellular functions, such as proliferation, apoptosis, regulation of the NF-kB pathway, endosomal recycling and the innate immune ...

    Abstract Tripartite motif-containing protein 27 (TRIM27/also called RFP) is a multifunctional ubiquitin E3 ligase involved in numerous cellular functions, such as proliferation, apoptosis, regulation of the NF-kB pathway, endosomal recycling and the innate immune response. TRIM27 interacts directly with TANK-binding kinase 1 (TBK1) and regulates its stability. TBK1 in complex with autophagy receptors is recruited to ubiquitin chains assembled on the mitochondrial outer membrane promoting mitophagy. Here, we identify TRIM27 as an autophagy substrate, depending on ATG7, ATG9 and autophagy receptors for its lysosomal degradation. We show that TRIM27 forms ubiquitylated cytoplasmic bodies that co-localize with autophagy receptors. Surprisingly, we observed that induced expression of EGFP-TRIM27 in HEK293 FlpIn TRIM27 knockout cells mediates mitochondrial clustering. TRIM27 interacts with autophagy receptor SQSTM1/p62, and the TRIM27-mediated mitochondrial clustering is facilitated by SQSTM/p62. We show that phosphorylated TBK1 is recruited to the clustered mitochondria. Moreover, induced mitophagy activity is reduced in HEK293 FlpIn TRIM27 knockout cells, while re-introduction of EGFP-TRIM27 completely restores the mitophagy activity. Inhibition of TBK1 reduces mitophagy in HEK293 FlpIn cells and in the reconstituted EGFP-TRIM27-expressing cells, but not in HEK293 FlpIn TRIM27 knockout cells. Altogether, these data reveal novel roles for TRIM27 in mitophagy, facilitating mitochondrial clustering via SQSTM1/p62 and mitophagy via stabilization of phosphorylated TBK1 on mitochondria.
    MeSH term(s) Humans ; Autophagy/physiology ; DNA-Binding Proteins/metabolism ; HEK293 Cells ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitophagy/physiology ; Nuclear Proteins/metabolism ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Sequestosome-1 Protein/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Tripartite Motif Proteins/metabolism
    Chemical Substances DNA-Binding Proteins ; Nuclear Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Sequestosome-1 Protein ; TBK1 protein, human (EC 2.7.11.1) ; TRIM27 protein, human ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Tripartite Motif Proteins
    Language English
    Publishing date 2022-09-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.16628
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: 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)

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  5. Article ; Online: TRIM32, but not its muscular dystrophy-associated mutant, positively regulates and is targeted to autophagic degradation by p62/SQSTM1.

    Overå, Katrine Stange / Garcia-Garcia, Juncal / Bhujabal, Zambarlal / Jain, Ashish / Øvervatn, Aud / Larsen, Kenneth Bowitz / Deretic, Vojo / Johansen, Terje / Lamark, Trond / Sjøttem, Eva

    Journal of cell science

    2019  Volume 132, Issue 23

    Abstract: The tripartite motif (TRIM) proteins constitute a family of ubiquitin E3 ligases involved in a multitude of cellular processes, including protein homeostasis and autophagy. TRIM32 is characterized by six protein-protein interaction domains termed NHL, ... ...

    Abstract The tripartite motif (TRIM) proteins constitute a family of ubiquitin E3 ligases involved in a multitude of cellular processes, including protein homeostasis and autophagy. TRIM32 is characterized by six protein-protein interaction domains termed NHL, various point mutations in which are associated with limb-girdle-muscular dystrophy 2H (LGMD2H). Here, we show that TRIM32 is an autophagy substrate. Lysosomal degradation of TRIM32 was dependent on ATG7 and blocked by knockout of the five autophagy receptors p62 (also known as SQSTM1), NBR1, NDP52 (also known as CALCOCO2), TAX1BP1 and OPTN, pointing towards degradation by selective autophagy. p62 directed TRIM32 to lysosomal degradation, while TRIM32 mono-ubiquitylated p62 on lysine residues involved in regulation of p62 activity. Loss of TRIM32 impaired p62 sequestration, while reintroduction of TRIM32 facilitated p62 dot formation and its autophagic degradation. A TRIM32
    MeSH term(s) Autophagy/genetics ; Autophagy/physiology ; HEK293 Cells ; HeLa Cells ; Humans ; Immunoprecipitation ; Muscular Dystrophies/genetics ; Muscular Dystrophies/metabolism ; Muscular Dystrophies, Limb-Girdle/genetics ; Muscular Dystrophies, Limb-Girdle/metabolism ; Protein Binding ; Sequestosome-1 Protein/genetics ; Sequestosome-1 Protein/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Tripartite Motif Proteins/genetics ; Tripartite Motif Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances SQSTM1 protein, human ; Sequestosome-1 Protein ; Transcription Factors ; Tripartite Motif Proteins ; TRIM32 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2019-12-02
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.236596
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: 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 14: Show issues

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