NDLI: Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1.

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Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhang, Tianlong Péli-Gulli, Marie-Pierre Yang, Hui De Virgilio, Claudio Ding, Jianping
Description	Country affiliation: China Author Affiliation: Zhang T ( State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China.)
Abstract	The yeast EGO complex, consisting of Gtr1, Gtr2, Ego1, and Ego3, localizes to the endosomal and vacuolar membranes and plays a pivotal role in cell growth and autophagy regulation through relaying amino acid signals to activate TORC1. Here, we report the crystal structures of a wild-type and a mutant form of Saccharomyces cerevisiae Ego3. Ego3 assumes a homodimeric structure similar to that of the mammalian MP1-p14 heterodimer and the C-terminal domains of the yeast Gtr1-Gtr2 heterodimer, both of which function in TORC1 signaling. Structural and genetic data demonstrate that the unique dimer conformation of Ego3 is essential for the integrity and function of the EGO complex. Structural and functional data also identify a potential binding site for Gtr1-Gtr2. These results suggest a structural conservation of the protein components involved in amino acid signaling to TORC1 and reveal structural insights into the molecular mechanism of Ego3 function in TORC1 signaling.
File Format	HTM / HTML
ISSN	09692126
Issue Number	12
Volume Number	20
e-ISSN	18784186
Journal	Structure
Language	English
Publisher	Elsevier
Publisher Date	2012-12-05
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology Membrane Proteins Chemistry Monomeric Gtp-binding Proteins Metabolism Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Transcription Factors Amino Acid Sequence Amino Acid Substitution Binding Sites Crystallography, X-ray Hydrophobic And Hydrophilic Interactions Genetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-directed Protein Binding Protein Interaction Domains And Motifs Protein Structure, Quaternary Protein Structure, Secondary Protein Transport Growth & Development Structural Homology, Protein Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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Dynamic relocation of the TORC1–Gtr1/2–Ego1/2/3 complex is regulated by Gtr1 and Gtr2

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Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1.

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Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1.