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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

ATG8 Atg8p

Atg8, Aut7, GATE-16, Apg8
mouse homolog may function as a soluble transport factor and/or a GABA(A) receptor linker [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: LC3, Ubiquitin, CAN, GABARAP, V1a
Papers on Atg8
Lipid Geometry and Bilayer Curvature Modulate LC3/GABARAP-Mediated Model Autophagosomal Elongation.
Alonso et al., Bilbao, Spain. In Biophys J, Feb 2016
Here, we used two minimal reconstituted systems (enzymatic and chemical conjugation) to compare the ability of human ATG8 homologs (LC3, GABARAP, and GATE-16) to mediate membrane fusion.
Moderate stress responses and specific changes in polyamine metabolism characterize Scots pine somatic embryogenesis.
Vuosku et al., Oulu, Finland. In Tree Physiol, Feb 2016
Cellular PA contents and the expression of the PA metabolism genes arginine decarboxylase (ADC), spermidine synthase (SPDS), thermospermine synthase (ACL5) and diamine oxidase (DAO) were analyzed, as well as the expression of catalase (CAT), DNA repair genes (RAD51, KU80) and autophagy-related genes (ATG5, ATG8) throughout the induction of somatic embryo formation in Scots pine SE cultures.
The two Dictyostelium autophagy eight proteins, ATG8a and ATG8b, associate with the autophagosome in succession.
Eichinger et al., Köln, Germany. In Eur J Cell Biol, Jan 2016
Autophagy 8 (ATG8, in mammals LC3), a well-established marker of autophagy, is covalently linked to phosphatidylethanolamine on the autophagic membrane during autophagosome formation.
Activation of ULK Kinase and Autophagy by GABARAP Trafficking from the Centrosome Is Regulated by WAC and GM130.
Tooze et al., London, United Kingdom. In Mol Cell, Jan 2016
GABARAP, unlipidated and lipidated, but not LC3B, GABARAPL1, and GATE-16, specifically promotes ULK kinase activation dependent on the ULK1 LIR motif, elucidating a unique non-hierarchical role for GABARAP in starvation-induced activation of autophagy.
Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.
Zhang et al., Beijing, China. In Mol Cell, Jan 2016
Multicellular organisms have multiple homologs of the yeast ATG8 gene, but the differential roles of these homologs in autophagy during development remain largely unknown.
SLC27A4 regulate ATG4B activity and control reactions to chemotherapeutics-induced autophagy in human lung cancer cells.
Guo et al., Bozhou, China. In Tumour Biol, Jan 2016
ATG4B, a cysteine protease required for autophagy, cleaves the C-terminal amino acid of ATG8 family proteins to reveal a C-terminal glycine which is necessary for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to autophagosome precursor membranes.
Eat or be eaten: The autophagic plight of inactive 26S proteasomes.
Vierstra et al., Madison, United States. In Autophagy, Nov 2015
Removal of inactive complexes is instead mediated by the proteasomal ubiquitin receptor RPN10, which can simultaneously bind both ubiquitinated proteasomes and lipidated ATG8 lining autophagic membranes.
The functional and pathologic relevance of autophagy proteases.
López-Otín et al., In J Clin Invest, 2015
This process is coordinated by complex molecular systems, including the ATG8 ubiquitin-like conjugation system and the ATG4 cysteine proteases, which are implicated in the formation, elongation, and fusion of these autophagic vesicles.
Toxic metals and autophagy.
Bhattacharya et al., India. In Chem Res Toxicol, 2014
It is noted that metals/metalloids and nanoparticles prefer ATG8/LC3 as a potent inducer of autophagy in several cell lines or animal cells.
ATG8 localization in apicomplexan parasites: apicoplast and more?
Sahani et al., Tokyo, Japan. In Autophagy, 2014
Recent studies demonstrated that, in the apicomplexan parasites Plasmodium (malaria parasites) and Toxoplasma, ATG8 localizes to the apicoplast, a unique nonphotosynthetic plastid with 4 limiting membranes.
Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy.
Kimmelman et al., Boston, United States. In Nature, 2014
Like known cargo receptors, nuclear receptor coactivator 4 (NCOA4) was highly enriched in autophagosomes, and associated with ATG8 proteins that recruit cargo-receptor complexes into autophagosomes.
In vitro assays of lipidation of Mammalian atg8 homologs.
Kominami et al., Tokyo, Japan. In Curr Protoc Cell Biol, 2013
Mammalian Atg8 homologs (Atg8s) including LC3, GABARAP, and GATE-16, are also ubiquitin-like modifiers.
The autophagy-related protein kinase Atg1 interacts with the ubiquitin-like protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formation.
Ohsumi et al., Yokohama, Japan. In J Biol Chem, 2012
mutations in the Atg1 AIM cause a significant defect in autophagy, without affecting the functions of Atg1 implicated in triggering autophagosome formation
Ume6 transcription factor is part of a signaling cascade that regulates autophagy.
Klionsky et al., Ann Arbor, United States. In Proc Natl Acad Sci U S A, 2012
Ume6 is a negative regulator of ATG8 transcription, which acts along with a histone deacetylase complex including Sin3 and Rpd3 to regulate Atg8 levels
Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers.
Dikic et al., Frankfurt am Main, Germany. In Mol Cell Biol, 2012
identified 14 TBC domain-containing Rab GAPs that bind directly to ATG8 modifiers and that colocalize with LC3-positive autophagy membranes in cells
Identification of HSP90 as a new GABARAPL1 (GEC1)-interacting protein.
Delage-Mourroux et al., Besançon, France. In Biochimie, 2012
Data demonstrate that HSP90 interacts and protects GABARAPL1 from its degradation by the proteasome.
Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8.
Song et al., Seoul, South Korea. In Nat Struct Mol Biol, 2011
The structure of the C-terminal domain of Atg7 in complex with Atg8 shows the mode of dimerization and mechanism of recognition of Atg8.
ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death.
Debnath et al., San Francisco, United States. In Cell, 2010
ATG3 is the E2-like enzyme necessary for ATG8/LC3 lipidation during autophagy.
Network organization of the human autophagy system.
Harper et al., Boston, United States. In Nature, 2010
The six ATG8 orthologues in humans (MAP1LC3/GABARAP proteins) interact with a cohort of 67 proteins, with extensive binding partner overlap between family members, and frequent involvement of a conserved surface on ATG8 proteins known to interact with LC3-interacting regions in partner proteins.
Autophagy genes are essential for dauer development and life-span extension in C. elegans.
Levine et al., New York City, United States. In Science, 2003
Dauer formation is associated with increased autophagy and also requires C. elegans orthologs of the yeast autophagy genes APG1, APG7, APG8, and AUT10.
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