Popelka Hana, Klionsky Daniel J
a Life Sciences Institute; University of Michigan ; Ann Arbor , MI USA.
Autophagy. 2015 Nov 2;11(11):1953-1955. doi: 10.1080/15548627.2015.1087635.
ULK1 and ATG13 assemble with RB1CC1/FIP200 and ATG101 to form a macroautophagy (hereafter autophagy) induction (ULK1) complex in higher eukaryotes. The yeast counterpart, the Atg1 complex, is comprised of Atg1 and Atg13 (ULK1 and ATG13 homologs), Atg17 (a proposed functional homolog of RB1CC1), and either the Atg101 subunit (in Schizosaccharomyces pombe) or the Atg29-Atg31 heterodimer (in Saccharomyces cerevisiae). With mutual exclusivity of, and no detectable homology between, the Atg29-Atg31 dimer and Atg101, knowledge about the roles of these proteins in autophagy induction is an important piece in the puzzle of understanding the molecular mechanism of autophagy initiation. A recent study reporting the structure of the S. pombe homolog Atg101 bound to the Atg13 domain is a notable contribution to this knowledge (see the punctum in this issue of the journal).
在高等真核生物中，ULK1和ATG13与RB1CC1/FIP200和ATG101组装形成一个巨自噬（以下简称自噬）诱导（ULK1）复合体。酵母中的对应物，即Atg1复合体，由Atg1和Atg13（ULK1和ATG13的同源物）、Atg17（一种推测的RB1CC1功能同源物）以及Atg101亚基（在粟酒裂殖酵母中）或Atg29-Atg31异二聚体（在酿酒酵母中）组成。由于Atg29-Atg31二聚体和Atg101之间相互排斥且无明显同源性，了解这些蛋白质在自噬诱导中的作用是理解自噬起始分子机制这一难题中的重要一环。最近一项报道粟酒裂殖酵母同源物Atg101与Atg13结构域结合的研究对此知识做出了显著贡献（见本期杂志中的亮点文章）。
