Topic
EGO complex
About: EGO complex is a research topic. Over the lifetime, 16 publications have been published within this topic receiving 1259 citations.
Papers
TL;DR: It is reported that the yeast Rag GTPase homolog Gtr1, a component of the vacuolar-membrane-associated EGO complex (EGOC), interacts with and activates TORC1 in an amino-acid-sensitive manner and is regulated by the conserved guanine nucleotide exchange factor (GEF) Vam6.
472 citations
TL;DR: It is demonstrated that the EGO complex, in conjunction with TOR, positively regulates microautophagy, thus counterbalancing the massive rapamycin-induced, macroautophagic-mediated membrane influx toward the vacuolar membrane.
353 citations
TL;DR: It is found that the leucyl-tRNA synthetase (LeuRS) Cdc60 interacts with the Rag GTPase Gtr1 of the EGOC in a leucine-dependent manner and is disrupted by the engagement of CDC60 in editing mischarged tRNA(Leu).
353 citations
TL;DR: Ego1, which mediates membrane-anchoring of EGOC via lipid modifications that it acquires while traveling through the trans-Golgi network, is separately sorted to vacuoles and perivacuolar endosomes and critically relies on a division of labor between spatially sequestered populations of TORC1.
121 citations
TL;DR: The previously uncharacterized Ycr075w-a/Ego2 protein is identified as an additional EGOC component that is required for the integrity and localization of the heterodimeric Gtr1-Gtr2 GTPases, equivalent to mammalian Rag G TPases, which support a model in which the EGO-TC acts as a scaffold for Rag GTPase in TORC1 signaling.
Abstract: The target of rapamycin complex 1 (TORC1) integrates various hormonal and nutrient signals to regulate cell growth, proliferation, and differentiation. Amino acid-dependent activation of TORC1 is mediated via the yeast EGO complex (EGOC) consisting of Gtr1, Gtr2, Ego1, and Ego3. Here, we identify the previously uncharacterized Ycr075w-a/Ego2 protein as an additional EGOC component that is required for the integrity and localization of the heterodimeric Gtr1-Gtr2 GTPases, equivalent to mammalian Rag GTPases. We also report the crystal structure of the Ego1-Ego2-Ego3 ternary complex (EGO-TC) at 2.4 A resolution, in which Ego2 and Ego3 form a heterodimer flanked along one side by Ego1. Structural data also reveal the structural conservation of protein components between the yeast EGO-TC and the human Ragulator, which acts as a GEF for Rag GTPases. Interestingly, however, artificial tethering of Gtr1-Gtr2 to the vacuolar membrane is sufficient to activate TORC1 in response to amino acids even in the absence of the EGO-TC. Our structural and functional data therefore support a model in which the EGO-TC acts as a scaffold for Rag GTPases in TORC1 signaling.
82 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 1 |
| 2019 | 1 |
| 2018 | 2 |
| 2017 | 2 |
| 2015 | 5 |
| 2012 | 2 |