Articles producció científica> Medicina i Cirurgia

GNIP1 E3 ubiquitin ligase is a novel player in regulating glycogen metabolism in skeletal muscle

  • Identification data

    Identifier: imarina:3415906
    Authors:
    Montori-Grau MPedreira-Casahuga RBoyer-Díaz ZLassot IGarcía-Martínez COrozco ACebrià JOsorio-Conles OChacón MVendrell JVázquez-Carrera MDesagher SJiménez-Chillarón JGómez-Foix A
    Abstract:
    Glycogenin-interacting protein 1 (GNIP1) is a tripartite motif (TRIM) protein with E3 ubiquitin ligase activity that interacts with glycogenin. These data suggest that GNIP1 could play a major role in the control of glycogen metabolism. However, direct evidence based on functional analysis remains to be obtained.The aim of this study was 1) to define the expression pattern of glycogenin-interacting protein/Tripartite motif containing protein 7 (GNIP/TRIM7) isoforms in humans, 2) to test their ubiquitin E3 ligase activity, and 3) to analyze the functional effects of GNIP1 on muscle glucose/glycogen metabolism both in human cultured cells and in vivo in mice.We show that GNIP1 was the most abundant GNIP/TRIM7 isoform in human skeletal muscle, whereas in cardiac muscle only TRIM7 was expressed. GNIP1 and TRIM7 had autoubiquitination activity in vitro and were localized in the Golgi apparatus and cytosol respectively in LHCN-M2 myoblasts. GNIP1 overexpression increased glucose uptake in LHCN-M2 myotubes. Overexpression of GNIP1 in mouse muscle in vivo increased glycogen content, glycogen synthase (GS) activity and phospho-GSK-3?/? (Ser21/9) and phospho-Akt (Ser473) content, whereas decreased GS phosphorylation in Ser640. These modifications led to decreased blood glucose levels, lactate levels and body weight, without changing whole-body insulin or glucose tolerance in mouse.GNIP1 is an ubiquitin ligase with a markedly glycogenic effect in skeletal muscle.Copyright © 2018 Elsevier Inc. All rights reserved.
  • Others:

    Author, as appears in the article.: Montori-Grau M; Pedreira-Casahuga R; Boyer-Díaz Z; Lassot I; García-Martínez C; Orozco A; Cebrià J; Osorio-Conles O; Chacón M; Vendrell J; Vázquez-Carrera M; Desagher S; Jiménez-Chillarón J; Gómez-Foix A
    Department: Medicina i Cirurgia
    URV's Author/s: Vendrell Ortega, Juan José
    Keywords: Trim7: trim7 isoform 4 Synthase kinase-3 Skeletal muscle Protein Gnip1: trim7 isoform 1 Glycogen metabolism Glucose-uptake Adenovirus-mediated transfer Activation skeletal muscle gnip1: trim7 isoform 1 glycogen metabolism
    Abstract: Glycogenin-interacting protein 1 (GNIP1) is a tripartite motif (TRIM) protein with E3 ubiquitin ligase activity that interacts with glycogenin. These data suggest that GNIP1 could play a major role in the control of glycogen metabolism. However, direct evidence based on functional analysis remains to be obtained.The aim of this study was 1) to define the expression pattern of glycogenin-interacting protein/Tripartite motif containing protein 7 (GNIP/TRIM7) isoforms in humans, 2) to test their ubiquitin E3 ligase activity, and 3) to analyze the functional effects of GNIP1 on muscle glucose/glycogen metabolism both in human cultured cells and in vivo in mice.We show that GNIP1 was the most abundant GNIP/TRIM7 isoform in human skeletal muscle, whereas in cardiac muscle only TRIM7 was expressed. GNIP1 and TRIM7 had autoubiquitination activity in vitro and were localized in the Golgi apparatus and cytosol respectively in LHCN-M2 myoblasts. GNIP1 overexpression increased glucose uptake in LHCN-M2 myotubes. Overexpression of GNIP1 in mouse muscle in vivo increased glycogen content, glycogen synthase (GS) activity and phospho-GSK-3?/? (Ser21/9) and phospho-Akt (Ser473) content, whereas decreased GS phosphorylation in Ser640. These modifications led to decreased blood glucose levels, lactate levels and body weight, without changing whole-body insulin or glucose tolerance in mouse.GNIP1 is an ubiquitin ligase with a markedly glycogenic effect in skeletal muscle.Copyright © 2018 Elsevier Inc. All rights reserved.
    Thematic Areas: Saúde coletiva Odontología Nutrição Medicina iii Medicina ii Medicina i Interdisciplinar General medicine Farmacia Engenharias ii Enfermagem Endocrinology, diabetes and metabolism Endocrinology & metabolism Endocrinology Educação física Ciências biológicas iii Ciências biológicas ii Ciências biológicas i Ciência de alimentos Biotecnología Antropologia / arqueologia
    licence for use: https://creativecommons.org/licenses/by/3.0/es/
    ISSN: 00260495
    Author's mail: juanjose.vendrell@urv.cat
    Author identifier: 0000-0002-6994-6115
    Record's date: 2024-09-07
    Papper version: info:eu-repo/semantics/acceptedVersion
    Licence document URL: https://repositori.urv.cat/ca/proteccio-de-dades/
    Papper original source: Metabolism-Clinical And Experimental. 83 177-187
    APA: Montori-Grau M; Pedreira-Casahuga R; Boyer-Díaz Z; Lassot I; García-Martínez C; Orozco A; Cebrià J; Osorio-Conles O; Chacón M; Vendrell J; Vázquez-Car (2018). GNIP1 E3 ubiquitin ligase is a novel player in regulating glycogen metabolism in skeletal muscle. Metabolism-Clinical And Experimental, 83(), 177-187. DOI: 10.1016/j.metabol.2018.02.005
    Entity: Universitat Rovira i Virgili
    Journal publication year: 2018
    Publication Type: Journal Publications
  • Keywords:

    Endocrinology,Endocrinology & Metabolism,Endocrinology, Diabetes and Metabolism
    Trim7: trim7 isoform 4
    Synthase kinase-3
    Skeletal muscle
    Protein
    Gnip1: trim7 isoform 1
    Glycogen metabolism
    Glucose-uptake
    Adenovirus-mediated transfer
    Activation
    skeletal muscle
    gnip1: trim7 isoform 1
    glycogen metabolism
    Saúde coletiva
    Odontología
    Nutrição
    Medicina iii
    Medicina ii
    Medicina i
    Interdisciplinar
    General medicine
    Farmacia
    Engenharias ii
    Enfermagem
    Endocrinology, diabetes and metabolism
    Endocrinology & metabolism
    Endocrinology
    Educação física
    Ciências biológicas iii
    Ciências biológicas ii
    Ciências biológicas i
    Ciência de alimentos
    Biotecnología
    Antropologia / arqueologia
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