Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling

Author:

de Araujo Mariana E. G.1ORCID,Naschberger Andreas2ORCID,Fürnrohr Barbara G.2ORCID,Stasyk Taras1ORCID,Dunzendorfer-Matt Theresia2ORCID,Lechner Stefan2ORCID,Welti Stefan2ORCID,Kremser Leopold3,Shivalingaiah Giridhar2ORCID,Offterdinger Martin4,Lindner Herbert H.3ORCID,Huber Lukas A.15ORCID,Scheffzek Klaus2ORCID

Affiliation:

1. Division of Cell Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.

2. Division of Biological Chemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.

3. Division of Clinical Biochemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.

4. Division of Neurobiochemistry-Biooptics, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.

5. Austrian Drug Screening Institute, 6020 Innsbruck, Austria.

Abstract

Structure of human mTORC1 components The mTORC1 (mechanistic target of rapamycin complex 1) complex garners much attention as a signaling hub that coordinates input from growth-factor receptors and nutrient availability with metabolism and cell growth and proliferation. de Araujo et al. report the crystal structure of the LAMTOR (or “Ragulator”) complex that helps assemble mTORC1 at the lysosomal membrane for activation. The structure and functional studies reveal how LAMTOR1 wraps around the other subunits to hold them in place and interacts with the Rag guanosine triphosphatases in the complex. Science , this issue p. 377

Funder

Austrian Science Fund

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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