Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 19, Pages 7826-7831Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1013800108
Keywords
lysosomal storage disease
Categories
Funding
- National Science Foundation [31030043, 30971484]
- 973 Program [2010CB833704, 2011CB910100]
- Tsinghua University [2010THZ0, 2009THZ03071]
- NIH [GM079431]
- Division of Intramural Research of the National Institute of Allergy and Infectious Diseases, NIH, Department of Health and Human Services
Ask authors/readers for more resources
Autophagy is a conserved cellular process to degrade and recycle cytoplasmic components. During autophagy, lysosomes fuse with an autophagosome to form an autolysosome. Sequestered components are degraded by lysosomal hydrolases and presumably released into the cytosol by lysosomal efflux permeases. Following starvation-induced autophagy, lysosome homeostasis is restored by autophagic lysosome reformation (ALR) requiring activation of the target of rapamycin (TOR) kinase. Spinster (Spin) encodes a putative lysosomal efflux permease with the hallmarks of a sugar transporter. Drosophila spin mutants accumulate lysosomal carbohydrates and enlarged lysosomes. Here we show that defects in spin lead to the accumulation of enlarged autolysosomes. We find that spin is essential for mTOR reactivation and lysosome reformation following prolonged starvation. Further, we demonstrate that the sugar transporter activity of Spin is essential for ALR.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available