You are currently viewing the editor's summary.
View Full TextLog in to view the full text
AAAS login provides access to Science for AAAS members, and access to other journals in the Science family to users who have purchased individual subscriptions.
Register for free to read this article
As a service to the community, this article is available for free. Existing users log in.
More options
Download and print this article for your personal scholarly, research, and educational use.
Buy a single issue of Science for just $15 USD.
Sensing Lysosomal Status
Lysosomes clear cells of damaged organelles, cellular debris, and internalized materials. Lysosomal biogenesis requires the transcription factor TFEB, and Roczniak-Ferguson et al. investigated the mechanisms by which lysosomal status controlled the activity of TFEB. They found that TFEB interacted with mTOR (mechanistic target of rapamycin), a kinase that localizes to lysosomes. The mTOR-dependent phosphorylation of TFEB caused TFEB to interact with 14-3-3 proteins, which led to the retention of the transcription factor in the cytoplasm. When lysosomal function was inhibited, TFEB no longer interacted with mTOR, was dephosphorylated, and translocated to the nucleus. Thus, the localization (and thus activity) of TFEB is determined by mTOR-mediated phosphorylation, which in turn reflects lysosomal status.
