Kabeya Yukiko, Kawamata Tomoko, Suzuki Kuninori, Ohsumi Yoshinori
Division of Molecular Cell Biology, National Institute for Basic Biology, Myodaiji 38, Okazaki 444-8585, Japan.
Biochem Biophys Res Commun. 2007 May 4;356(2):405-10. doi: 10.1016/j.bbrc.2007.02.150. Epub 2007 Mar 7.
Autophagy is the bulk degradation of cytosolic materials in lysosomes/vacuoles of eukaryotic cells. In the yeast Saccharomyces cerevisiae, 17 Atg proteins are known to be involved in autophagosome formation. Genome wide analyses have shown that Atg17 interacts with numerous proteins. Further studies on these interacting proteins may provide further insights into membrane dynamics during autophagy. Here, we identify Cis1/Atg31 as a protein that exhibits similar phenotypes to Atg17. ATG31 null cells were defective in autophagy and lost viability under starvation conditions. Localization of Atg31 to pre-autophagosomal structures (PAS) was dependent on Atg17. Coimmunoprecipitation experiments indicated that Atg31 interacts with Atg17. Together, Atg31 is a novel protein that, in concert with Atg17, is required for proper autophagosome formation.
自噬是真核细胞溶酶体/液泡中胞质物质的大量降解过程。在酿酒酵母中,已知有17种自噬相关蛋白(Atg蛋白)参与自噬体的形成。全基因组分析表明,Atg17与众多蛋白质相互作用。对这些相互作用蛋白的进一步研究可能会为自噬过程中的膜动力学提供更深入的见解。在此,我们鉴定出Cis1/Atg31是一种与Atg17表现出相似表型的蛋白质。Atg31基因缺失的细胞在自噬方面存在缺陷,并且在饥饿条件下丧失活力。Atg31定位于自噬前体结构(PAS)依赖于Atg17。免疫共沉淀实验表明Atg31与Atg17相互作用。总之,Atg31是一种新的蛋白质,它与Atg17协同作用,是正常自噬体形成所必需的。