S
Sonia M. Scaria
Researcher at Massachusetts Institute of Technology
Publications - 12
Citations - 2650
Sonia M. Scaria is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: GTPase & mTORC1. The author has an hindex of 7, co-authored 9 publications receiving 2004 citations.
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Journal ArticleDOI
Sestrin2 is a leucine sensor for the mTORC1 pathway
Rachel L. Wolfson,Lynne Chantranupong,Robert A. Saxton,Kuang Shen,Sonia M. Scaria,Jason R. Cantor,David M. Sabatini +6 more
TL;DR: In this paper, it was shown that leucine, but not arginine, disrupts the Sestrin2-GATOR2 interaction with a dissociation constant of 20 micromolar.
Journal ArticleDOI
The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway
Lynne Chantranupong,Sonia M. Scaria,Robert A. Saxton,Melanie P. Gygi,Kuang Shen,Gregory A. Wyant,Timothy C. Wang,J. Wade Harper,Steven P. Gygi,David M. Sabatini +9 more
TL;DR: In this article, it was shown that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1.
Journal ArticleDOI
The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1.
Lynne Chantranupong,Rachel L. Wolfson,Jose M. Orozco,Robert A. Saxton,Sonia M. Scaria,Liron Bar-Peled,Eric Spooner,Marta Isasa,Steven P. Gygi,David M. Sabatini +9 more
TL;DR: The Sestrins are identified as GATOR2-interacting proteins that regulate the amino-acid-sensing branch of the mTORC1 pathway, which requires GATOR1 and the Rag GTPases, and the SestRins regulate the localization of m TORC1 in response to amino acids.
Journal ArticleDOI
SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway
Xin Gu,Jose M. Orozco,Robert A. Saxton,Kendall J. Condon,Grace Y. Liu,Patrycja A. Krawczyk,Sonia M. Scaria,J. Wade Harper,Steven P. Gygi,David M. Sabatini +9 more
TL;DR: In this article, the methyl donor S-adenosylmethionine (SAM) disrupts the SAMTOR-GATOR1 complex by binding directly to SAMTOR with a dissociation constant of approximately 7 μM.
Journal ArticleDOI
KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to regulate mTORC1
Rachel L. Wolfson,Lynne Chantranupong,Gregory A. Wyant,Xin Gu,Jose M. Orozco,Kuang Shen,Kendall J. Condon,Sabrina Petri,Jibril Fetu Kedir,Sonia M. Scaria,Monther Abu-Remaileh,Wayne N. Frankel,David M. Sabatini +12 more
TL;DR: KICSTOR is a lysosome-associated negative regulator of mTORC1 signalling, which, like GATOR1, is mutated in human disease and Notably, several KICstOR components are mutated in neurological diseases associated with mutations that lead to hyperactive mTORc1 signalling.