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de Araujo, Mariana E. G.; Naschberger, Andreas; Fürnrohr, Barbara G.; Stasyk, Taras; Dunzendorfer-Matt, Theresia; Lechner, Stefan; Welti, Stefan; Kremser, Leopold; Shivalingaiah, Giridhar; Offterdinger, Martin; Lindner, Herbert H.; Huber, Lukas A.; Scheffzek, Klaus

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

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  • Media type: E-Article
  • Title: Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling
  • Contributor: de Araujo, Mariana E. G.; Naschberger, Andreas; Fürnrohr, Barbara G.; Stasyk, Taras; Dunzendorfer-Matt, Theresia; Lechner, Stefan; Welti, Stefan; Kremser, Leopold; Shivalingaiah, Giridhar; Offterdinger, Martin; Lindner, Herbert H.; Huber, Lukas A.; Scheffzek, Klaus
  • Published: American Association for the Advancement of Science (AAAS), 2017
  • Published in: Science, 358 (2017) 6361, Seite 377-381
  • Language: English
  • DOI: 10.1126/science.aao1583
  • ISSN: 0036-8075; 1095-9203
  • Origination:
  • Footnote:
  • Description: 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