Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1
Abstract
The mTORC1 protein kinase is a complex of proteins that functions to regulate growth and metabolism. Activity of mTORC1 is sensitive to the abundance of amino acids, but how the sensing of amino acids is coupled to the control of mTORC1 has been unclear. Wang et al. searched for predicted membrane proteins that interacted with regulators of mTORC1. They identified a protein currently known only as SLC38A9. Interaction of SLC38A9 with mTORC1 regulators was sensitive to the presence of amino acids. SLC38A9 has sequence similarity to amino acid transporters. Effects of modulation of SLC38A9 in cultured human cells indicate that it may be the sensor that connects the abundance of arginine and leucine to mTORC1 activity.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Jan 09, 2015
- Source ID
- 10.1126/science.1257132
Entities
People
- Bernardo L. Sabatini
- Choah Kim
- Christoph Straub
- David M. Sabatini
- Elizabeth D. Yuan
- Gregory A Wyant
- J. Park
- Kuang Shen
- Liron Bar-peled
- Lynne Chantranupong
- Molly E. Plovanich
- Rachel L. Wolfson
- Roberto Zoncu
- Shuyu Wang
- Tim Wang
- Tony D. Jones
- William Comb
- Zhi-yang Tsun
Organizations
- German Academic Exchange Service
- Harvard Medical School
- Howard Hughes Medical Institute
- Koch Institute for Integrative Cancer Research at MIT
- Massachusetts Institute of Technology
- National Institutes of Health
- United States Department of Defense