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

Montori-Grau, Marta; Pedreira-Casahuga, Robert; Boyer-Díaz, Zoé; Lassot, Irina; Garcı́a-Martı́nez, Cèlia; Orozco, Anna; Cebrià, Judith; Osorio-Conles, Óscar; Chacón, Matilde R.; Vendrell, Joan; Vázquez‐Carrera, Manuel; Desagher, Solange; Jiménez-Chillarón, Josep C.; Gómèz-Foix, Anna M.

doi:10.1016/j.metabol.2018.02.005

Cited by 25 publications

(23 citation statements)

References 43 publications

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“…TRIM7 may play a role in determining ZIKV tissue tropism in vivo, because ZIKV replicated to lower titers in brain and reproductive tissues (uterus and testis) as compared with other tissues of Trim7 −/− mice and as compared with WT littermate controls [ 17 ••]. Cell fractionation experiments suggested that TRIM7 and its E2-Ub conjugase UbcH5a [ 127 , 128 ] co-localize in the endoplasmic reticulum (ER) compartment in ZIKV infected cells, although TRIM7 can also re-localize to the Golgi [ 17 ••, 129 ], suggesting that TRIM7 may be hijacked by ZIKV-E during maturation in the Golgi or during replication in the ER (Fig. 3c #3 ).…”

Section: Trim Proteins In Pathogenesismentioning

confidence: 99%

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TRIM Proteins in Host Defense and Viral Pathogenesis

Giraldo

Hage

Tol

et al. 2020

Curr Clin Micro Rpt

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Purpose of Review Tripartite motif (TRIM) proteins are a large group of E3 ubiquitin ligases involved in different cellular functions. Of special interest are their roles in innate immunity, inflammation, and virus replication. We discuss novel roles of TRIM proteins during virus infections that lead to increased pathogenicity. Recent Findings TRIM proteins regulate different antiviral and inflammatory signaling pathways, mostly by promoting ubiquitination of important factors including pattern recognition receptors, adaptor proteins, kinases, and transcription factors that are involved in type I interferon and NF-κB pathways. Therefore, viruses have developed mechanisms to target TRIMs for immune evasion. New evidence is emerging indicating that viruses have the ability to directly use TRIMs and the ubiquitination process to enhance the viral replication cycle and cause increased pathogenesis. A new report on TRIM7 also highlights the potential pro-viral role of TRIMs via ubiquitination of viral proteins and suggests a novel mechanism by which ubiquitination of virus envelope protein may provide determinants of tissue and species tropism. Summary TRIM proteins have important functions in promoting host defense against virus infection; however, viruses have adapted to evade TRIM-mediated immune responses and can hijack TRIMs to ultimately increase virus pathogenesis. Only by understanding specific TRIM-virus interactions and by using more in vivo approaches can we learn how to harness TRIM function to develop therapeutic approaches to reduce virus pathogenesis.

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Section: Trim Proteins In Pathogenesismentioning

confidence: 99%

“…TRIM7 in known to be involved in some important biological processes including tumor cell proliferation and glycogen metabolism [ 129 , 133 ]. TRIM7 has also been shown to act as an E3 ligase mediating K63-linked polyubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization [ 127 ].…”

Section: Trim Proteins In Pathogenesismentioning

confidence: 99%

TRIM Proteins in Host Defense and Viral Pathogenesis

Giraldo

Hage

Tol

et al. 2020

Curr Clin Micro Rpt

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“…TRIM7 has at least four isoforms in humans, with isoform 1 and isoform 4 containing a functional RING domain, while isoforms 2 and 3 do not. TRIM7 isoforms 1 and 4 are the most commonly studied and display different expression pattern in muscular tissues and cells (31). We generated stable HeLa-CD300lf cells overexpressing TRIM7 isoform 1 or isoform 4 (Fig.…”

Section: Generation Of Crispra Libraries In Hela-cd300lf Cellsmentioning

confidence: 99%

Identification of Antinorovirus Genes in Human Cells Using Genome-Wide CRISPR Activation Screening

Orchard

Sullender

Dunlap

et al. 2019

J Virol

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Noroviruses (NoVs) are a leading cause of gastroenteritis worldwide, yet host factors that restrict NoV replication are not well understood. Here, we use a CRISPR activation genome-wide screening to identify host genes that can inhibit murine norovirus (MNoV) replication in human cells. Our screens identified with high confidence 49 genes that can inhibit MNoV infection when overexpressed. A significant number of these genes are in interferon and immune regulation signaling networks, but surprisingly, the majority of the genes identified are neither associated with innate or adaptive immunity nor associated with any antiviral activity. Confirmatory studies of eight of the genes validate the initial screening data. Mechanistic studies on TRIM7 demonstrated a conserved role of the molecule in mouse and human cells in restricting MNoV in a step of infection after viral entry. Furthermore, we demonstrate that two isoforms of TRIM7 have differential antiviral activity. Taken together, these data provide a resource for understanding norovirus biology and demonstrate a robust methodology for identifying new antiviral molecules. IMPORTANCE Norovirus is one of the leading causes of food-borne illness worldwide. Despite its prevalence, our understanding of norovirus biology is limited due to the difficulty in growing human norovirus in vitro and a lack of an animal model. Murine norovirus (MNoV) is a model norovirus system because MNoV replicates robustly in cell culture and in mice. To identify host genes that can restrict norovirus replication when overexpressed, we performed genome-wide CRISPR activation screens to induce gene overexpression at the native locus through recruitment of transcriptional activators to individual gene promoters. We found 49 genes that could block murine norovirus replication in human cells. Several of these genes are associated with classical immune signaling pathways, while many of the molecules we identified have not been previously associated with antiviral activity. Our data are a resource for those studying noroviruses, and we provide a robust approach to identify novel antiviral genes.

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“…Blocking this pathway might result in insulin resistance with impaired glucose metabolism [ 16 , 17 ]. On the contrary, activation of the AKT/GSK3β pathway leads to improvement of glucose metabolism [ 18 ]. The AKT/FOXO pathway is another pathway that participates in glucose metabolism regulation.…”

Section: Introductionmentioning

confidence: 99%

Chlorogenic Acid Targeting of the AKT PH Domain Activates AKT/GSK3β/FOXO1 Signaling and Improves Glucose Metabolism

Gao

et al. 2018

Nutrients

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Chlorogenic acid (CGA), a bioactive component in the human diet, is reported to exert beneficial effects on the regulation of glucose metabolism. This study was designed to investigate the specific target of CGA, and explore its underlying mechanisms. Beneficial effects of CGA in glucose metabolism were confirmed in insulin-treated human hepatocarcinoma HepG2 cells. Protein fishing, via CGA-modified functionalized magnetic microspheres, demonstrated the binding of CGA with protein kinase B (AKT). Immunofluorescence using a CGA molecular probe further demonstrated the co-localization of CGA with AKT. A competitive combination test and hampering of AKT membrane translocation showed that CGA might bind to the pleckstrin homology (PH) domain of AKT. The specific binding did not lead to the membrane translocation to phosphatidylinositol (3,4,5)-trisphosphate (PIP3), but directly activated the phosphorylation of AKT on Ser-473, induced the phosphorylation of the downstream molecules, glycogen synthase kinase 3β (GSK3β) and forkhead box O1 (FOXO1), and improved glucose metabolism. Collectively, our data demonstrate that CGA exerts regulatory effects on glucose metabolism via direct targeting the PH domain of AKT. This study clarifies the mechanism of the potential benefits of nutrients containing CGA in the complementary therapy of glucose metabolism disorders.

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

Abstract: GNIP1 is an ubiquitin ligase with a markedly glycogenic effect in skeletal muscle.

Cited by 25 publications

References 43 publications

TRIM Proteins in Host Defense and Viral Pathogenesis

TRIM Proteins in Host Defense and Viral Pathogenesis

Identification of Antinorovirus Genes in Human Cells Using Genome-Wide CRISPR Activation Screening

Chlorogenic Acid Targeting of the AKT PH Domain Activates AKT/GSK3β/FOXO1 Signaling and Improves Glucose Metabolism

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