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The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy*
Results indicate that the Atg12-Atg5 conjugate is a ubiquitin-protein ligase (E3)-like enzyme for Atg8-PE conjugation reaction, distinctively promoting protein-lipid conjugations.
Atg8‐family interacting motif crucial for selective autophagy
The structure of Atg4B–LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy
The crystal structures of catalytically inert human Atg4 B (HsAtg4B) in complex with processed and unprocessed forms of LC3, a mammalian orthologue of yeast Atg8, are reported.
Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses.
Structural basis of target recognition by Atg8/LC3 during selective autophagy
- N. Noda, H. Kumeta, F. Inagaki
- Biology, ChemistryGenes to cells : devoted to molecular & cellular…
- 1 December 2008
The results show the fundamental mechanism that allows Atg8 homologues, in association with WXXL‐containing proteins, to capture specific cargo molecules, thereby endowing isolation membranes and/or their assembly machineries with target selectivity.
Tor2 Directly Phosphorylates the AGC Kinase Ypk2 To Regulate Actin Polarization
It is proposed that Ypk protein kinases are direct and essential targets ofTORC2, coupling TORC2 to the cell integrity cascade.
Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site
- M. Mazhab-Jafari, C. Marshall, M. Ikura
- BiologyProceedings of the National Academy of Sciences
- 4 May 2015
A mechanism of K-RAS4B autoinhibition by membrane sequestration of its effector-binding site, which can be disrupted by disease-associated mutations is revealed, opening new avenues for therapeutic strategies to target oncogenic K- RAS through stabilizing autoinhibitory interactions with the membrane.
Structural basis of starvation-induced assembly of the autophagy initiation complex
Dephosphorylation of specific serines in Atg13 enhanced its interaction with not only Atg1 but also Atg17, and this promotes PAS assembly and autophagy progression.
Mechanisms of Autophagy.
This review describes from a structural-biological point of view the structure, interaction, and molecular roles of Atg proteins, especially those in the Atg1 complex and in theAtg conjugation systems.
Identification of Ser-386 of Interferon Regulatory Factor 3 as Critical Target for Inducible Phosphorylation That Determines Activation*
- Mitsuaki Mori, M. Yoneyama, Takashi Ito, Kiyohiro Takahashi, F. Inagaki, T. Fujita
- Biology, ChemistryJournal of Biological Chemistry
- 12 March 2004
The results strongly suggest that Ser-386 is the target of the IRF-3 kinase and critical determinant for the activation of IRf-3.