4.8 Editorial Material

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

Journal

AUTOPHAGY
Volume 12, Issue 6, Pages 1061-1062

Publisher

TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2015.1091143

Keywords

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

Categories

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available