对LC3脂化过程中E2-E3相互作用的结构见解。
Structural insights into E2-E3 interaction for LC3 lipidation.
作者信息
Metlagel Zoltan, Otomo Chinatsu, Ohashi Kazuto, Takaesu Giichi, Otomo Takanori
机构信息
Department of Integrative Structural and Computational Biology; The Scripps Research Institute; La Jolla, CA USA.
Department of Molecular Bacteriology and Immunology; Graduate School of Medicine; University of the Ryukyus; Okinawa, Japan.
出版信息
Autophagy. 2014 Mar;10(3):522-3. doi: 10.4161/auto.27594. Epub 2014 Jan 9.
The members of the LC3/Atg8 family of proteins are covalently attached to phagophore and autophagosomal membranes. At the last step of the LC3 lipidation cascade, LC3 is transferred from the E2 enzyme ATG3 to phosphatidylethanolamine (PE). This transfer is stimulated by the ATG12-ATG5-ATG16L1 E3 complex, but the mechanism is not fully understood. We recently found that ATG12 of the E3 binds to a short sequence in the flexible region (FR) of ATG3 with high affinity, and that this interaction is critical for E2-E3 complex formation. These findings, together with detailed structural analyses of this interaction, define the properties of ATG12 and provide new insights of how LC3 transfer begins with ATG3 recruitment by ATG12.
LC3/Atg8蛋白家族的成员共价连接于吞噬泡膜和自噬体膜。在LC3脂化级联反应的最后一步，LC3从E2酶ATG3转移至磷脂酰乙醇胺（PE）。这种转移受到ATG12-ATG5-ATG16L1 E3复合体的刺激，但其机制尚未完全明确。我们最近发现，E3的ATG12以高亲和力结合于ATG3柔性区域（FR）中的一段短序列，且这种相互作用对于E2-E3复合体的形成至关重要。这些发现，连同对这种相互作用的详细结构分析，确定了ATG12的特性，并为LC3转移如何通过ATG12招募ATG3起始提供了新见解。
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