Recruitment of folliculin to lysosomes supports the amino acid–dependent activation of Rag GTPases

Authors:
Constance S. Petit, Agnes Roczniak-Ferguson, and Shawn M. Ferguson
In:
Source: J Cell Biol
Publication Date: (2013)
Issue: 202(7): 1107-1122
Research Area:
Cancer Research/Cell Biology
Cells used in publication:
HeLa
Species: human
Tissue Origin: cervix
Platform:
Nucleofector® I/II/2b
Experiment
Device used: Nucleofector I/II/2b Cell type: Hela M (stably transfected with transcription factor EB-GFP fusion) System: CRISPR/Cas9 Cell number: 1x10e6/100 µl Substrate amount (co-transfected): 300 pmol of oligonucleotide for repair 2.5 µg each of the Cas9 and gRNA plasmids Solution: R Program A-24 Summary (Lonza): The authors have used the CRISPR Technology in combination with Nucleofection to insert a 3xHA epitope tag to their gene of interest allowing for better protein detection by immunofluorescence (for localization studies).
Abstract
Birt-Hogg-Dubé syndrome, a human disease characterized by fibrofolliculomas (hair follicle tumors) as well as a strong predisposition toward the development of pneumothorax, pulmonary cysts, and renal carcinoma, arises from loss-of-function mutations in the folliculin (FLCN) gene. In this study, we show that FLCN regulates lysosome function by promoting the mTORC1-dependent phosphorylation and cytoplasmic sequestration of transcription factor EB (TFEB). Our results indicate that FLCN is specifically required for the amino acid-stimulated recruitment of mTORC1 to lysosomes by Rag GTPases. We further demonstrated that FLCN itself was selectively recruited to the surface of lysosomes after amino acid depletion and directly bound to RagA via its GTPase domain. FLCN-interacting protein 1 (FNIP1) promotes both the lysosome recruitment and Rag interactions of FLCN. These new findings define the lysosome as a site of action for FLCN and indicate a critical role for FLCN in the amino acid-dependent activation of mTOR via its direct interaction with the RagA/B GTPases.