ATG14 Antibody

1. Knockdown of ATG14 protein leds to decreased autophagy and chemoresistance of melphalan-resistant myeloma cells PMID:30121664
2. This study identifies an unexpected role for PtdIns(4,5)P2 signaling in the regulation of ATG14 complex and autophagy. PMID:27621469
3. These data provide evidence for additional roles of Atg2A and Atg14L in the formation of early autophagosomal membranes and also in lipid metabolism. PMID:24776541
4. we found that ATG14 interacted with Ulk1 and LC3, and knock down of Ulk1 prevented the lipidation of LC3 and autophagy in HeLa-ATG14 cells. We also identified a phosphatidylethanolamine (PE) binding region in ATG14, and the addition of Ulk1 to Hela-ATG14 cells decreased the ATG14-PE interaction. PMID:28069524
5. polar BECN2 CCD interface residues result in a metastable homodimer, facilitating dissociation, but enable better interactions with polar ATG14 residues stabilizing the BECN2:ATG14 heterodimer. PMID:28218432
6. use circular dichroism and small-angle X-ray scattering (SAXS) to show that the ATG14 coiled-coil domain (CCD) is significantly disordered but becomes more helical in the BECN1:ATG14 heterodimer, although it is less well-folded than the BECN1 CCD homodimer PMID:27383850
7. These results define a key molecular event for the starvation-induced activation of the ATG14-containing PtdIns3K complex by ULK1. PMID:27046250
8. data suggest an autophagy-specific membrane fusion mechanism in which oligomeric ATG14 directly binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion PMID:25686604
9. Cisplatin upregulated Barkor protein levels of the Saos-2 cell line. PMID:24337183
10. Atg14 is critical in controlling an autophagy-dependent phosphorylation of beclin-1. We map novel phosphorylation sites to serines 90 and 93 and demonstrate that phosphorylation at these sites is necessary for maximal autophagy. PMID:23878393
11. Our findings reveal that Atg14L, previously considered to be solely a Beclin 1-binding autophagy protein, plays a novel role in the late stage of endocytic trafficking in conjunction with Snapin PMID:22797916
12. Anaplasma actively induces autophagy by secreting Ats-1 that hijacks the Beclin 1-Atg14L autophagy initiation pathway likely to acquire host nutrients for its growth PMID:23197835
13. Atg14 is a new target gene of FoxOs and the core clock machinery, and this gene plays an important role in hepatic lipid metabolism PMID:22992773
14. analysis of how the Beclin1 coiled-coil domain interface regulates homodimer and heterodimer formation with Atg14L and UVRAG PMID:22314358
15. Data suggest that the Atg14L-dependent appearance of phosphatidylinositol 3-phosphate in the endoplasmic reticulum makes this organelle the platform for autophagosome formation. PMID:20713597
16. These results suggest that mammalian cells have at least two distinct class III PI3-kinase complexes, and that beclin 1 interacts distinctly with mammalian Atg14 and UVRAG in two of these complexes. PMID:18843052
17. study defines a regulatory signaling pathway mediated by Barkor (KIAA0831) that positively controls autophagy through Beclin 1 PMID:19050071
18. Two Beclin 1 associated proteins, Atg14L and Rubicon, were identified. PMID:19270696
19. Barkor/KIAA0831 functions as an autophagy targeting factor for Beclin 1 and the class III PI3 kinase. Barkor and UVRAG form two distinct protein complexes with the core class III PI3 kinase. Barkor is a functional ortholog of yeast Atg14. PMID:19050071

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HGNC: 19962

UNIGENE: Hs.414809

KEGG: hsa:22863

STRING: 9606.ENSP00000247178

OMIM: 613515