Asset Details
Do you wish to reserve the book?
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H⁺-ATPase
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H⁺-ATPase
Do you wish to request the book?
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H⁺-ATPase
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H⁺-ATPase
2011
Overview
The mTOR complex 1 (mTORC1) protein kinase is a master growth regulator that is stimulated by amino acids. Amino acids activate the Rag guanosine triphosphatases (GTPases), which promote the translocation of mTORC1 to the lysosomal surface, the site of mTORC1 activation. We found that the vacuolar H⁺-adenosine triphosphatase ATPase (v-ATPase) is necessary for amino acids to activate mTORC1. The v-ATPase engages in extensive amino acid-sensitive interactions with the Ragulator, a scaffolding complex that anchors the Rag GTPases to the lysosome. In a cell-free system, ATP hydrolysis by the v-ATPase was necessary for amino acids to regulate the v-ATPase-Ragulator interaction and promote mTORC1 translocation. Results obtained in vitro and in human cells suggest that amino acid signaling begins within the lysosomal lumen. These results identify the v-ATPase as a component of the mTOR pathway and delineate a lysosome-associated machinery for amino acid sensing.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Anchors
/ Animals
/ Biological and medical sciences
/ Cell structures and functions
/ Cytosol
/ Enzymes
/ Esters
/ Fundamental and applied biological sciences. Psychology
/ GTP Phosphohydrolases - metabolism
/ Humans
/ Kinases
/ Lumens
/ Mechanistic Target of Rapamycin Complex 1
/ Molecular and cellular biology
/ Proteins
/ TOR Serine-Threonine Kinases
/ Vacuolar Proton-Translocating ATPases - metabolism
/ vacuoles
We currently cannot retrieve any items related to this title. Kindly check back at a later time.