Research TopicsGenomes and Genes | ATG16SummaryGene Symbol: ATG16 Description: Atg16p Alias: APG15, APG16, CVT11, SAP18, Atg16p Species: Saccharomyces cerevisiae S288c Top Publications
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- Kuma A, Mizushima N, Ishihara N, Ohsumi Y. Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem. 2002;277:18619-25 pubmed..the yeast Saccharomyces cerevisiae, the Apg12-Apg5 conjugate further interacts with a small coiled-coil protein, Apg16. The Apg12-Apg5 and Apg16 are localized in the cytosol and pre-autophagosomal structures and play an essential ..
- Mizushima N, Noda T, Ohsumi Y. Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. EMBO J. 1999;18:3888-96 pubmed..These results suggest that the Apg12p-Apg5p conjugate requires Apg16p to accomplish its role in the autophagy pathway, and Apg16p is a key molecule as a linker to form the Apg12p-Apg5p-Apg16p multimer. ..
- Kanki T, Wang K, Baba M, Bartholomew C, Lynch Day M, Du Z, et al. A genomic screen for yeast mutants defective in selective mitochondria autophagy. Mol Biol Cell. 2009;20:4730-8 pubmed publisher..Accordingly, we have named this gene ATG33. The new mutants identified in this analysis will provide a useful foundation for researchers interested in the study of mitochondrial homeostasis and quality control. ..
- Fujioka Y, Noda N, Matsushita M, Ohsumi Y, Inagaki F. Crystallization of the coiled-coil domain of Atg16 essential for autophagy. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008;64:1046-8 pubmed publisherb>Atg16 is a scaffold protein that interacts with Atg12-Atg5 protein conjugates via its N-terminal domain and self-assembles via its coiled-coil domain, thus forming a multimeric Atg12-Atg5-Atg16 complex that is essential for autophagy...
- Hanada T, Ohsumi Y. Structure-function relationship of Atg12, a ubiquitin-like modifier essential for autophagy. Autophagy. 2005;1:110-8 pubmed..Gel filtration analysis suggests that F154 plays a critical role in the assembly of a functional Atg12-Atg5.Atg16 complex that is requisite for autophagosome formation.
- Kaufmann A, Beier V, Franquelim H, Wollert T. Molecular mechanism of autophagic membrane-scaffold assembly and disassembly. Cell. 2014;156:469-81 pubmed publisher..protein Atg8 to phosphatidylethanolamine (Atg8-PE) in autophagic membranes by a complex consisting of Atg16 and the Atg12-Atg5 conjugate...
- Mijaljica D, Prescott M, Devenish R. A late form of nucleophagy in Saccharomyces cerevisiae. PLoS ONE. 2012;7:e40013 pubmed publisher..Moreover, the inhibition of LN in some mutants is accompanied by alterations in nuclear morphology. ..
- Fracchiolla D, Sawa Makarska J, Zens B, Ruiter A, Zaffagnini G, Brezovich A, et al. Mechanism of cargo-directed Atg8 conjugation during selective autophagy. elife. 2016;5: pubmed publisher..Atg19, Atg34 and the human p62, Optineurin and NDP52 cargo receptors interact with the E3-like enzyme Atg12~Atg5-Atg16, which stimulates Atg8 conjugation...
- Romanov J, Walczak M, Ibiricu I, Schüchner S, Ogris E, Kraft C, et al. Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16 complex during autophagosome formation. EMBO J. 2012;31:4304-17 pubmed publisher..The conserved Atg5-Atg12/Atg16 complex is essential for autophagosome formation...
- Noda N, Fujioka Y, Hanada T, Ohsumi Y, Inagaki F. Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation. EMBO Rep. 2013;14:206-11 pubmed publisher..Rather, Atg12 functions as a binding module for Atg3, the E2 enzyme for Atg8, thus endowing Atg5 with the ability to interact with Atg3 to facilitate Atg8 lipidation. ..