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Yasemin Sancak
Researcher at Harvard University
Publications - 40
Citations - 15164
Yasemin Sancak is an academic researcher from Harvard University. The author has contributed to research in topics: Uniporter & Mitochondrion. The author has an hindex of 24, co-authored 31 publications receiving 13473 citations. Previous affiliations of Yasemin Sancak include Broad Institute & University of Göttingen.
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Journal ArticleDOI
The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
Yasemin Sancak,Timothy R. Peterson,Yoav D. Shaul,Robert A. Lindquist,Carson C. Thoreen,Liron Bar-Peled,David M. Sabatini,David M. Sabatini +7 more
TL;DR: It is found that the Rag proteins—a family of four related small guanosine triphosphatases (GTPases)—interact with mTORC1 in an amino acid–sensitive manner and are necessary for the activation of the m TORC1 pathway by amino acids.
Journal ArticleDOI
Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
Yasemin Sancak,Liron Bar-Peled,Roberto Zoncu,Andrew L. Markhard,Shigeyuki Nada,David M. Sabatini +5 more
TL;DR: It is shown that amino acids induce the movement of m TORC1 to lysosomal membranes, where the Rag proteins reside, and Rag-Ragulator-mediated translocation of mTORC1 is the key event in amino acid signaling to mtorC1.
Journal ArticleDOI
Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
Joshua M. Baughman,Fabiana Perocchi,Fabiana Perocchi,Hany S. Girgis,Hany S. Girgis,Molly Plovanich,Molly Plovanich,Casey A. Belcher-Timme,Casey A. Belcher-Timme,Yasemin Sancak,Yasemin Sancak,X. Robert Bao,X. Robert Bao,Laura Strittmatter,Laura Strittmatter,Olga Goldberger,Olga Goldberger,Roman L. Bogorad,Victor Koteliansky,Vamsi K. Mootha,Vamsi K. Mootha +20 more
TL;DR: Genome phylogenetic profiling, genome-wide RNA co-expression analysis and organelle-wide protein coexpression analysis are used to predict proteins functionally related to MICU1, establishing MCU as an essential component of the mitochondrial Ca2+ uniporter.
Journal ArticleDOI
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H+-ATPase
TL;DR: In this article, the v-ATPase engages in extensive amino acid-sensitive interactions with the Ragulator, a scaffolding complex that anchors the Rag GTPases to the lysosome.
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H+-ATPase
TL;DR: The v-ATPase is identified as a component of the mTOR pathway and a lysosome-associated machinery for amino acid sensing is delineated, suggesting that amino acid signaling begins within the lysOSomal lumen.