SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1

The mechanistic target of rapamycin (serine/threonine kinase) complex 1 (MTORC1) acts as a crucial regulator of cellular metabolism by integrating growth factor presence, energy and nutrient availability to coordinate anabolic and catabolic processes, and controls cell growth and proliferation. Amin...

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Main Authors:	Rebsamen, Manuele, Superti-Furga, Giulio
Format:	Online
Language:	English
Published:	Taylor & Francis 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4922434/

id	pubmed-4922434
recordtype	oai_dc
spelling	pubmed-49224342016-07-08 SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1 Rebsamen, Manuele Superti-Furga, Giulio Autophagic Puncta The mechanistic target of rapamycin (serine/threonine kinase) complex 1 (MTORC1) acts as a crucial regulator of cellular metabolism by integrating growth factor presence, energy and nutrient availability to coordinate anabolic and catabolic processes, and controls cell growth and proliferation. Amino acids are critical for MTORC1 activation, but the molecular mechanisms involved in sensing their presence are just beginning to be understood. We recently reported that the previously uncharacterized amino acid transporter SLC38A9 is a member of the lysosomal sensing machinery that signals amino acid availability to MTORC1. SLC38A9 is the first component of this complex shown to physically engage amino acids, suggesting a role at the core of the amino acid-sensing mechanism. Taylor & Francis 2015-10-02 /pmc/articles/PMC4922434/ /pubmed/26431368 http://dx.doi.org/10.1080/15548627.2015.1091143 Text en © 2016 The Author(s). Published with license by Taylor & Francis http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Rebsamen, Manuele Superti-Furga, Giulio
spellingShingle	Rebsamen, Manuele Superti-Furga, Giulio SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1
author_facet	Rebsamen, Manuele Superti-Furga, Giulio
author_sort	Rebsamen, Manuele
title	SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1
title_short	SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1
title_full	SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1
title_fullStr	SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1
title_full_unstemmed	SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1
title_sort	slc38a9: a lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls mtorc1
description	The mechanistic target of rapamycin (serine/threonine kinase) complex 1 (MTORC1) acts as a crucial regulator of cellular metabolism by integrating growth factor presence, energy and nutrient availability to coordinate anabolic and catabolic processes, and controls cell growth and proliferation. Amino acids are critical for MTORC1 activation, but the molecular mechanisms involved in sensing their presence are just beginning to be understood. We recently reported that the previously uncharacterized amino acid transporter SLC38A9 is a member of the lysosomal sensing machinery that signals amino acid availability to MTORC1. SLC38A9 is the first component of this complex shown to physically engage amino acids, suggesting a role at the core of the amino acid-sensing mechanism.
publisher	Taylor & Francis
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4922434/
_version_	1613600109359005696

SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1

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