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ATG12 autophagy related 12 homolog

Atg12, Apg12
Autophagy is a process of bulk protein degradation in which cytoplasmic components, including organelles, are enclosed in double-membrane structures called autophagosomes and delivered to lysosomes or vacuoles for degradation. ATG12 is the human homolog of a yeast protein involved in autophagy (Mizushima et al., 1998 [PubMed 9852036]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Atg5, LC3, Atg7, Ubiquitin, Atg8
Papers using Atg12 antibodies
Polyethylenimine, a cost-effective transfection reagent.
Kampinga Harm, In PLoS ONE, 2005
... JNK1/2 (#9255), Akt-T308 (#4056) and total antibodies for LC3b (#2775), Beclin-1 (#3738), p38 (#9212) and ATG12 (#2010) were from Cell signaling Technology ...
Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
Peppelenbosch M P et al., In Cell Death & Disease, 1991
... (Tyr108/182), p-SHP-2 (Tyr542), p-PTEN (Ser380), p-mTOR (Ser2448), p-p70S6K (Thr389), p-S6 (Ser235/236), Beclin-1, LC3BI/II, Atg5, Atg7, Atg12, anti-rabbit and anti-mouse peroxidase-conjugated antibodies were from Cell Signaling Technology (Beverly, MA, USA) ...
Papers on Atg12
Unique role for ATG5 in neutrophil-mediated immunopathology during M. tuberculosis infection.
Stallings et al., Saint Louis, United States. In Nature, Jan 2016
The involvement of autophagy has been defined based on studies in cultured cells where M. tuberculosis co-localizes with autophagy factors ATG5, ATG12, ATG16L1, p62, NDP52, BECN1 and LC3 (refs 2-6), stimulation of autophagy increases bacterial killing, and inhibition of autophagy increases bacterial survival.
BAG3 regulates total MAP1LC3B protein levels through a translational but not transcriptional mechanism.
Lavandero et al., Mainz, Germany. In Autophagy, Jan 2016
In some scenarios, the induction of autophagy is accompanied by increased levels of certain ATG mRNAs such as MAP1LC3B/LC3B, ATG5 or ATG12.
FGFR3/fibroblast growth factor receptor 3 inhibits autophagy through decreasing the ATG12-ATG5 conjugate, leading to the delay of cartilage development in achondroplasia.
Chen et al., Chongqing, China. In Autophagy, Dec 2015
Furthermore, we found that FGFR3 interacted with ATG12-ATG5 conjugate by binding to ATG5.
Atg7 in development and disease: panacea or Pandora's Box?
Xiong, Bethesda, United States. In Protein Cell, Oct 2015
Atg7 acts as an E1-like activating enzyme facilitating both microtubule-associated protein light chain 3 (LC3)-phosphatidylethanolamine and ATG12 conjugation.
Endoplasmic reticulum stress and autophagy participate in apoptosis induced by bortezomib in cervical cancer cells.
Zhang et al., Beijing, China. In Biotechnol Lett, Oct 2015
Bortezomib also induced the loss of the mitochondrial membrane potential, increased the level of ER stress-associated proteins GRP78, ATF4, and CCAAT-enhancer-binding protein homologous protein, and affected the expression of autophagy-related proteins; increasing the levels of LC3-II and ATG5-ATG12 and decreasing the level of p62.
ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late endosome function.
Debnath et al., San Francisco, United States. In Nat Cell Biol, Mar 2015
The ubiquitin-like molecule ATG12 is required for the early steps of autophagy.
ATG12-ATG3 connects basal autophagy and late endosome function.
Debnath et al., San Francisco, United States. In Autophagy, 2014
We recently identified a novel interaction between the ATG12-ATG3 conjugate and the ESCRT-associated protein PDCD6IP/Alix that promotes basal autophagy and endolysosomal trafficking.
Inhibition of HIF-1α Affects Autophagy Mediated Glycosylation in Oral Squamous Cell Carcinoma Cells.
Wang et al., Hangzhou, China. In Dis Markers, 2014
Short interfering RNA (siRNA) transfection blocked human ATG12 and ATG1.
Caffeine reduces hepatic lipid accumulation through regulation of lipogenesis and ER stress in zebrafish larvae.
Hou et al., Guangzhou, China. In J Biomed Sci, 2014
Moreover, caffeine treatment was associated with upregulation of lipid β-oxidation gene ACO and downregulation of lipogenesis-associated genes (SREBP1, ACC1, CD36 and UCP2), ER stress-associated genes (PERK, IRE1, ATF6 and BIP), the inflammatory cytokine genes (IL-1beta and TNF-alpha) and autophagy associated genes (ATG12 and Beclin-1).
Structural insights into E2-E3 interaction for LC3 lipidation.
Otomo et al., Los Angeles, United States. In Autophagy, 2014
This transfer is stimulated by the ATG12-ATG5-ATG16L1 E3 complex, but the mechanism is not fully understood.
Nondegradative role of Atg5-Atg12/ Atg16L1 autophagy protein complex in antiviral activity of interferon gamma.
Virgin et al., Saint Louis, United States. In Cell Host Microbe, 2012
Atg5-Atg12/Atg16L1 protein complex is required for IFNgamma-mediated host defense against murine norovirus infection.
Autophagy proteins LC3B, ATG5 and ATG12 participate in quality control after mitochondrial damage and influence lifespan.
Jendrach et al., Frankfurt am Main, Germany. In Autophagy, 2012
These data relate LC3B, ATG5 and ATG12 to mitochondrial quality control after oxidative damage, and to cellular longevity.
The autophagy protein Atg12 associates with antiapoptotic Bcl-2 family members to promote mitochondrial apoptosis.
Kimchi et al., Israel. In Mol Cell, 2012
The Atg12 is as a positive mediator of mitochondrial apoptosis and show that Atg12 directly regulates the apoptotic pathway by binding and inactivating prosurvival Bcl-2 family members, including Bcl-2 and Mcl-1.
Vaccinia virus leads to ATG12–ATG3 conjugation and deficiency in autophagosome formation.
Jin et al., United States. In Autophagy, 2011
Vaccinia virus actively disrupts the cellular autophagy through a novel molecular mechanism that is associated with aberrant LC3 lipidation and a direct conjugation between ATG12 and ATG3.
Atg16L2, a novel isoform of mammalian Atg16L that is not essential for canonical autophagy despite forming an Atg12–5-16L2 complex.
Fukuda et al., Sendai, Japan. In Autophagy, 2011
Despite forming the Atg12-Atg5-Atg16L2 complex, Atg16L2 is not recruited to phagophores and is mostly present in the cytosol.
Modification by ubiquitin-like proteins: significance in apoptosis and autophagy pathways.
Ntwasa et al., Johannesburg, South Africa. In Int J Mol Sci, 2011
Modifiers such as SUMO, ATG12, ISG15, FAT10, URM1, and UFM have been shown to modify proteins thus conferring functions related to programmed cell death, autophagy and regulation of the immune system.
ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death.
Debnath et al., San Francisco, United States. In Cell, 2010
ATG12, an ubiquitin-like modifier required for macroautophagy, has a single known conjugation target, another autophagy regulator called ATG5.
Role of the Apg12 conjugation system in mammalian autophagy.
Ohsumi et al., Kawaguchi, Japan. In Int J Biochem Cell Biol, 2003
The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes.
A ubiquitin-like system mediates protein lipidation.
Ohsumi et al., Okazaki, Japan. In Nature, 2000
Apg7 activates two different ubiquitin-like proteins, Apg12 (ref.
A protein conjugation system essential for autophagy.
Ohsumi et al., Okazaki, Japan. In Nature, 1998
The carboxy-terminal glycine residue of Apg12, a 186-amino-acid protein, is conjugated to a lysine at residue 149 of Apg5, a 294-amino-acid protein.
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