Related Experiment Video
Updated: Mar 31, 2026

Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles
Published on: October 18, 2024
The amino acid transporter SLC38A9 regulates MTORC1 and autophagy
Meiyan Jin1, Daniel J Klionsky1
1a Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology, University of Michigan ; Ann Arbor , MI USA.
Abstract:
The mechanistic target of rapamycin (serine/threonine kinase) complex 1 (MTORC1) is a master regulator of macroautophagy (hereafter autophagy) that responds to different environmental nutrients, including amino acids, glucose, and growth factors. The identity of the amino acid-sensing component of the MTORC1 machinery had remained elusive until a lysosomal low-affinity amino acid transporter, SLC38A9 (solute carrier family 38, member 9), was recently characterized as a novel component of the Ragulator-RRAG GTPase complex by 3 independent research groups.
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