Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway (Q24307790)

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26 January 2020

title

Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway (English)

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Late endosomal/lysosomal adaptor, MAPK and MTOR activator 1

26 January 2020

main subject

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Regulatory associated protein of MTOR complex 1

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Isoleucyl-tRNA synthetase 1

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mechanistic target of rapamycin kinase

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Ras related GTP binding C

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Ras related GTP binding B

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Ras related GTP binding D

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Leucyl-tRNA synthetase 1

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Methionyl-tRNA synthetase 1

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cellular response to leucine starvation

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author

Sung Ho Ryu

8

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26 January 2020

author name string

Jung Min Han

1

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26 January 2020

Seung Jae Jeong

2

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26 January 2020

Min Chul Park

3

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26 January 2020

Gyuyoup Kim

4

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26 January 2020

Nam Hoon Kwon

5

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26 January 2020

Hoi Kyoung Kim

6

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26 January 2020

Sang Hoon Ha

7

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26 January 2020

Sunghoon Kim

9

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26 January 2020

language of work or name

English

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publication date

15 March 2012

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26 January 2020

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26 January 2020

volume

149

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26 January 2020

page(s)

410-424

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26 January 2020

issue

2

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Regulation of amino acid-sensitive TOR signaling by leucine analogues in adipocytes

26 January 2020

cites work

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7 January 2021

mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events

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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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The two TORCs and Akt.

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Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers

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Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb

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7 January 2021

Structural and functional considerations of the aminoacylation reaction

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7 January 2021

The 'KMSKS' motif in tyrosyl-tRNA synthetase participates in the initial binding of tRNA(Tyr)

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7 January 2021

Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

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Regulation of TORC1 by Rag GTPases in nutrient response

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7 January 2021

Molecular mechanisms of mTOR-mediated translational control

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7 January 2021

Orthogonal use of a human tRNA synthetase active site to achieve multifunctionality

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The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation.

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Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases

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Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B

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Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1

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7 January 2021

The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex

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7 January 2021

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7 January 2021

Re-evaluating the roles of proposed modulators of mammalian target of rapamycin complex 1 (mTORC1) signaling

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7 January 2021

Mammalian target of rapamycin (mTOR): conducting the cellular signaling symphony

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7 January 2021

Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis

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7 January 2021

Rab7: a key to lysosome biogenesis

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7 January 2021

The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue

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7 January 2021

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Regulation of polypeptide chain initiation and activity of initiation factor eIF-2 in Chinese-hamster-ovary cell mutants containing temperature-sensitive aminoacyl-tRNA synthetases

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7 January 2021

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7 January 2021

The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1

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Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

789570

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26 January 2020

789570

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

789570

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22424946%20AND%20SRC:MED&resulttype=core&format=json