Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1-Reference-Cited by-同舟云学术

Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1

Published:2015-01-09 Issue:6218 Volume:347 Page:188-194
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Wang Shuyu¹²³⁴,Tsun Zhi-Yang¹²³⁴,Wolfson Rachel L.¹²³⁴,Shen Kuang¹²³⁴,Wyant Gregory A.¹²³⁴,Plovanich Molly E.⁵,Yuan Elizabeth D.¹²³⁴,Jones Tony D.¹²³⁴,Chantranupong Lynne¹²³⁴,Comb William¹²³⁴,Wang Tim¹²³⁴,Bar-Peled Liron¹²³⁴,Zoncu Roberto¹²³⁴,Straub Christoph⁶,Kim Choah¹²³⁴,Park Jiwon¹²³⁴,Sabatini Bernardo L.⁶,Sabatini David M.¹²³⁴

Affiliation:

1. Whitehead Institute for Biomedical Research and Massachusetts Institute of Technology, Department of Biology, 9 Cambridge Center, Cambridge, MA 02142, USA.

2. Howard Hughes Medical Institute, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

3. Koch Institute for Integrative Cancer Research, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.

4. Broad Institute of Harvard and Massachusetts Institute of Technology, 7 Cambridge Center, Cambridge, MA 02142, USA.

5. Harvard Medical School, 260 Longwood Avenue, Boston, MA 02115, USA.

6. Department of Neurobiology, Howard Hughes Medical Institute, Harvard Medical School, 220 Longwood Avenue, Boston, MA 02115, USA.

Abstract

Sensing amino acids at the lysosome 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. Science , this issue p. 188

Funder

NIH

Department of Defense

Howard Hughes Medical Institute

German Academic Exchange Service

National Defense Science and Engineering Graduate Fellowship

NSF Graduate Research Fellowship

American Cancer Society-Ellison Foundation Postdoctoral Fellowship

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary