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第四届中国结构生物学学术讨论会

作者： Tianlong Zhang Marie-Pierre Péli-Gulli Hui Yang claudio de virgilio Jianping Ding State Key Laboratory of Molecular Biology Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Division of Biochemistry Department of Biology University of Fribourg

The mammalian TOR（mTOR） and its orthologues are central regulators of cell growth, proliferation, and differentiation, and have been implicated in many diseases including cancers and diabetes. Amino acid levels are signaled to TORC1 via the EGO complex in yeast or the structurally orthologous ragulator complex in mammalian cells. 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. depletion of any of the EGOC components leads to failure in recovery from rapamycin-induced growth arrest and causes low TORC1 activity, indicating that these proteins play an important role in cell growth regulation upstream of TORC1. In line with this assumption, GTP-bound Gtr1 combines with GDP-bound Gtr2 to interact with and activate TORC1 via a still elusive mechanism. Analogous to the role of p18 in the Ragulator complex in higher eukaryotes, the N-myristoylated Ego1 may serve to properly tether Gtr1-Gtr2 to the vacuolar/lysosomal membrane for proper TORC1 activation, while the role of Ego3 in this process is still poorly understood. Here we report the crystal structures of a wild-type and a mutant form of S. 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.

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Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Egol in the EGO complex to activate TORC1

Ego3 functions as a homodimer to mediate the interaction bet...

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生命的分子机器及其调控网络——2012年全国生物化学与分子生物学学术大会

作者： Tianlong Zhang Marie-Pierre Pli-Gulli Hui Yang claudio de virgilio Jianping Ding State Key Laboratory of Molecular Biology Institute of Biochemistry and Cell BiologyShanghai Institutes for Biological SciencesChinese Academy of Sciences Division of Biochemistry Department of BiologyUniversity of FribourgCH-1700 FribourgSwitzerland

TORC1 integrates a variety of cell growth signals to regulate cell growth,proliferation,and *** yeast EGO complex(EGOC),consisting of Gtr1,Gtr2,Ego1/Meh1,and Ego3/Slm4,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 *** solved the crystal structures of a wild-type and a mutant form of S. cerevisiae Ego3 at 2.1 A and 2.6 A resolution,***3 assumes a homodimeric structure that displays

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

Ego3 functions as a homodimer to mediate the interaction bet...

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中国晶体学会第五届全国会员代表大会暨学术大会（大分子分会场）

TORC1 integratesa variety ofcell growth signalsto regulate cell growth,proliferation,*** yeast EGO complex(EGOC),consisting of Gtr1,Gtr2,Ego1/Meh1,and Ego3/Slm4,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 *** the crystal structures of a wild-type and a mutant form of *** Ego3 at 2.1? and 2.6?

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Structural insights into the Ragulator-and EGO-TC-mediated membrane tethering of the mTORC1-regulatory Rag GTPases

Structural insights into the Ragulator-and EGO-TC-mediated m...

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中国生物化学与分子生物学会2019年全国学术会议暨学会成立四十周年

作者： Tianlong Zhang Marie-Pierre Péli-Gulli Rong Wang Zhen Zhang claudio de virgilio Jianping Ding CAS Center for Excellence in Molecular Cell Science Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences University of Fribourg

The Rag/Gtr GTPases serve as a central module in the nutrient-sensing signaling network upstream of TORC1. In human, the nutrient-activated Rag heterodimer binds to mTORC1 to promote its recruitment to lysosomal membranes, where it is in a position to interact with the small GTPase Rheb that promotes its kinase activity. The Rag GTPases are recruited to lysosomes via the scaffold Ragulator/LAMTOR complex, consisting of p18, MP1, p14, HBXIP and C7 orf59. In yeast, Gtr1 and Gtr2 are orthologs of mammalian Rag GTPases, which also form a functional obligate heterodimer. The anchoring of Gtr1-Gtr2 to membranes depends on the Ego1-Ego2-Ego3 ternary complex(EGO-TC), resulting in an EGO-TC-Gtr1-Gtr2 complex(EGOC). Intriguingly, EGO-TC and human Ragulator share no obvious sequence similarities and also differ in their composition with respect to the number of known subunits. Here, we report the structures of Ragulator and EGOC. The functional roles of key residues involved in the assembly are validated by in vivo assays. Our structural and functional data combined demonstrate that Ragulator-Rag and EGOC are structurally conserved and that Ragulator and EGO-TC are essential to recruit Rag GTPase to membranes to ensure appropriate TORC1 activation.

关键词： mTORC1 crystal structure protein complex

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Left Ventricular Pacing in a Patient with a Mechanical Tricuspid Prosthesis and High Surgical Risk

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World Journal of Cardiovascular Diseases 2014年第12期4卷 567-569页

作者： Sergio Conti claudio Liotta Alfredo virgilio Corrado Tamburino Valeria Calvi Cardiology department Ferrarotto Hospital University of Catania Catania Italy

Transvenous endocardial pacemaker (PM) implantation is contraindicated in patients with a mechanical tricuspid prosthesis. These patients usually undergo epicardial lead implantation. This case shows the implant of left ventricular (LV) pacing lead through the coronary sinus (CS) in a patient with high surgical risk. A 77-year-old woman with slow atrial fibrillation, left anterior hemi-block and right bundle brunch block, who previously underwent surgical replacement of the mitral and tricuspid valves, was admitted for PM implantation. After 1 month, all the electric parameters were stable. To the best of our knowledge, this is the first Italian case reported of LV pacing in a patient with a mechanical tricuspid prosthesis. The use of LV pacing leads implanted through the CS provides a minimal invasive, safe and effective strategy of pacing in patients with a mechanical tricuspid prosthesis.

关键词： Pacemaker Tricuspid Valve Prosthesis

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