Format

Send to

Choose Destination
Autophagy. 2016 Jun 2;12(6):1061-2. doi: 10.1080/15548627.2015.1091143. Epub 2015 Oct 2.

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

Author information

1
a CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences , Vienna , Austria.
2
b Center for Physiology and Pharmacology, Medical University of Vienna , Vienna , Austria.

Abstract

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.

KEYWORDS:

MTOR; amino acid transport; cancer; metabolism; nutrient sensing; solute carrier proteins

PMID:
26431368
PMCID:
PMC4922434
DOI:
10.1080/15548627.2015.1091143
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Taylor & Francis Icon for PubMed Central
Loading ...
Support Center