Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex.
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GLIPR2 is an unusual nonsecreted CAP protein on the cytosolic endomembrane system.
"localizes to the cytosolic site of the endomembrane system in mammalian cells."
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GAPR-1 is N-myristoylated and associates strongly with Golgi membrane microdomains.
"GAPR-1 was shown to be myristoylated."
Cloning and characterization of a human novel gene C9orf19 encoding a conserved putative protein with an SCP-like extracellular protein domain.
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The GLIPR2 transcript is broadly expressed, with highest abundance in lung and peripheral leukocytes in the sampled panel.
"C9orf19 mRNA is expressed in a wide range of adult tissues as a single transcript, most abundantly in lung and peripheral blood leukocytes."
Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism.
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GLIPR2 forms dimers in vitro and in vivo.
"GAPR-1 may form dimers in vitro and in vivo, as determined"
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Conserved interface mutations increase the dimer population.
"mutagenesis of these conserved amino acid residues leads to a greatly increased"
Proteomic analysis of exosomes from human neural stem cells by flow field-flow fractionation and nanoflow liquid chromatography-tandem mass spectrometry.
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The study performed mass-spectrometric protein identification on morphologically confirmed neural-stem-cell exosome fractions.
"Exosomal lysates of each fraction were digested and analyzed using nanoflow"
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Interaction of GAPR-1 with lipid bilayers is regulated by alternative homodimerization.
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Inositol hexakisphosphate promotes a distinct GLIPR2 dimer conformation.
"phytic acid (inositol hexakisphosphate) induces dimerization of GAPR-1 in solution."
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A membrane-responsive dimer conformation tethers negatively charged liposomes.
"In the presence of negatively charged lipids, GAPR-1 caused a rapid and stable tethering of liposomes."
Identification of a candidate therapeutic autophagy-inducing peptide.
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GLIPR2 binds BECN1 residues 267-284 and negatively regulates autophagy.
"Taken together, our data indicate that GAPR-1 is a beclin 1-interacting protein that negatively regulates autophagy."
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Golgi-bound GLIPR2 may sequester inactive BECN1.
"Thus, GAPR-1 may function to tether beclin 1 in the Golgi apparatus (where it is inactive in autophagy)"
GLIPR-2 overexpression in HK-2 cells promotes cell EMT and migration through ERK1/2 activation.
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GLIPR2 overexpression induces EMT-like marker changes and migration in human HK-2 cells.
"Taken together, these results suggest that the high expression of GLIPR-2 in epithelial cells may promote an EMT."
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The EMT/migration phenotype requires ERK1/2 and GLIPR2 myristoylation in this model.
"However, p-ERK1/2 and EMT markers did not change in the non-myr GLIPR-2-transfected HK-2 cells."
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Hypoxia promotes epithelial--mesenchymal transition of hepatocellular carcinoma cells via inducing GLIPR-2 expression.
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GLIPR2 overexpression promotes, and GLIPR2 knockdown attenuates, ERK-dependent EMT, migration, and invasion in human HCC cells.
"These results revealed that suppression of GLIPR-2 expression in human HCC cells attenuated ERK1/2 activation and EMT-like process following by migration and invasion in response to hypoxia."
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The authors explicitly limit extrapolation of the cell-line results to intact organisms.
"However, further work is needed to determine the extrapolation of in vitro results to an in vivo situation."
Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1) forms amyloid-like fibrils by interaction with acidic phospholipids and inhibits Aβ aggregation.
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Purified GLIPR2 forms amyloid-like fibrils with negatively charged liposomes and inhibits Aβ peptide aggregation in vitro.
"GAPR-1 has the capability to form amyloid-like fibrils in the presence of liposomes containing negatively charged lipids."
The Golgi-Associated Plant Pathogenesis-Related Protein GAPR-1 Enhances Type I Interferon Signaling Pathway in Response to Toll-Like Receptor 4.
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IRAK1 phosphorylation of GAPR-1 promotes TMED7 binding and enhances TLR4-dependent IFN-beta and IL10 output.
"The phosphorylation of GAPR-1 promoted its interaction with TRAM-TRIF dependent inhibitor TMED7, and impaired TMED7-mediated disruption of the TRAM-TRIF complex to trigger IFN-β and the IL10 secretion."
Structural insights into the interaction of the conserved mammalian proteins GAPR-1 and Beclin 1, a key autophagy protein.
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Five conserved GLIPR2 groove residues are required for BECN1 binding.
"Mutation of the five conserved residues lining this groove, H54A/E86A/G102K/H103A/N138G, abrogates Beclin 1 binding."
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GLIPR2 dimerization and BECN1 binding are structurally antagonistic.
"dimeric GAPR-1 is unlikely to bind Beclin 1."
Zinc binding regulates amyloid-like aggregation of GAPR-1.
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Zinc binding regulates GLIPR2 oligomer and amyloid-like assembly in vitro.
"The Zn2+-induced conformational change was required for the formation of GAPR-1 oligomers and amyloid-like assemblies in the presence of heparin"
Metal ions and redox balance regulate distinct amyloid-like aggregation pathways of GAPR-1.
GLIPR2 is a negative regulator of autophagy and the BECN1-ATG14-containing phosphatidylinositol 3-kinase complex.
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GLIPR2 directly binds and inhibits the autophagy-initiating PtdIns3K-C1 lipid kinase complex.
"GLIPR2 binds to purified PtdIns3K-C1 and inhibits its in vitro lipid kinase activity."
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Human GLIPR2 knockout increases autophagic flux, and wild-type rescue reverses the phenotype.
"Thus, using four independent assays, we demonstrate that GLIPR2 negatively regulates autophagy in cultured cells."
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Glipr2-null mouse tissues show increased basal autophagic flux and PtdIns3K-C1 activity.
"Taken together, these data reveal increased autophagic flux and PtdIns3K-C1 activity in glipr2-/-mice, providing evidence that GLIPR2 functions as a negative regulator of autophagy in vivo."
Dynamic and Reversible Aggregation of the Human CAP Superfamily Member GAPR-1 in Protein Inclusions in Saccharomyces cerevisiae.
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Overexpressed human GLIPR2 forms dynamic, reversible cytosolic inclusions in a heterologous yeast model.
"These cytosolic inclusions are dynamic and reversible organelles that gradually increase during time of overexpression and decrease after promoter shut-off."
GAPR-1 Interferes with Condensate Formation of Beclin 1 in Saccharomyces cerevisiae.
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GLIPR2 suppresses BECN1 condensates through their known binding surfaces in a heterologous yeast co-expression model.
"co-expression of hGAPR-1-GFP and hBeclin 1-mCherry results in a strong reduction of hBeclin 1 condensates."
UniProt entry for human GLIPR2 (Q9H4G4)
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Reviewed UniProt records the Golgi membrane location, myristoylation, homodimerization, and caveolin-1 interaction.
"SUBUNIT: Homodimer. Interacts with CAV1."
Manual literature synthesis for human GLIPR2