Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling. (Q47764522)

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30 March 2020

title

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

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Mariana E G de Araujo

1

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Andreas Naschberger

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Barbara G Fürnrohr

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Taras Stasyk

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Theresia Dunzendorfer-Matt

30 March 2020

5

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Stefan Lechner

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Stefan Welti

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Giridhar Shivalingaiah

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Herbert H Lindner

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Klaus Scheffzek

13

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8

Leopold Kremser

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author name string

Martin Offterdinger

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language of work or name

English

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publication date

21 September 2017

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volume

358

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issue

6361

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page(s)

377-381

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Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1

30 March 2020

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Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids

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LAMTOR2 regulates dendritic cell homeostasis through FLT3-dependent mTOR signalling

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The late endosome/lysosome-anchored p18-mTORC1 pathway controls terminal maturation of lysosomes

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Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9

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SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1

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Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1

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The Dawn of the Age of Amino Acid Sensors for the mTORC1 Pathway

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Disruption of the Rag-Ragulator Complex by c17orf59 Inhibits mTORC1.

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Interactions between Kinase Scaffold MP1/p14 and Its Endosomal Anchoring Protein p18

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The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes.

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Identifiers

DOI

10.1126/SCIENCE.AAO1583

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28935770 AND SRC:MED&resulttype=core&format=json

30 March 2020

1 reference