ATG Systems from the Protein Structural Point of View

被引：62

作者：

Noda, Nobuo N. ^{[2
]}

Ohsumi, Yoshinori ^{[1
]}

Inagaki, Fuyuhiko ^{[2
]}

机构：

[1] Natl Inst Basic Biol, Mol Cell Biol Div, Okazaki, Aichi 4448585, Japan

[2] Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Biol Struct, Sapporo, Hokkaido 0010021, Japan

来源：

CHEMICAL REVIEWS | 2009年 / 109卷 / 04期

关键词：

PRE-AUTOPHAGOSOMAL STRUCTURE; VACUOLE TARGETING PATHWAY; MEMBRANE-TRANSPORT MODULATOR; RECEPTOR-ASSOCIATED PROTEIN; IN-VITRO RECONSTITUTION; E3 LIGASE ACTIVITY; SACCHAROMYCES-CEREVISIAE; CRYSTAL-STRUCTURE; CONJUGATING ENZYME; MAMMALIAN AUTOPHAGY;

D O I：

10.1021/cr800459r

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A study revealed that Atg proteins were responsible for autophagosome formations and showed the structures of Atg8 homologues and enzymes modifying Atg8. The autophagy-specific phosphatidylinositol 3-kinase complex produced phosphatidylinositol 3-phosphase and the localization of this complex were determined by Atg14. The crystal structure of S. cerevisiae Atg8 was determined as a complex with a peptide derived from Atg19, which was similar to mammalian homologues comprising the N-terminal helical domain and the C-terminal ubiquitin-like domain. It was observed that the Atg protein was made of various functional group like Atg1 kinase and its regulators, an autophagy-specific phosphatidylinositol 3-kinase complex, the integral membrane protein Atg9, and the Atg2-Atg18 complex. The structural study of Atg proteins provided an insight of mechanism of autophagasome formation.

引用

页码：1587 / 1598

页数：12

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