ArticleOpen biology2015
Lst4, the yeast Fnip1/2 orthologue, is a DENN-family protein.
Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Homogentisate 1,2-dioxygenase (HGD) gene variants, their analysis and genotype-phenotype correlations in the largest cohort of patients with AKU.European journal of human genetics : EJHG · 2019Trial
- Non-dikarya fungi share the TORC1 pathway with animals, not with Saccharomyces cerevisiae.Scientific reports · 2025Article
- Familial multiple discoid fibromas is linked to a locus on chromosome 5 including the FNIP1 gene.Journal of human genetics · 2023Article
- A pathogenic variant in theFrontiers in neuroscience · 2023Article
- The fission yeast FLCN/FNIP complex augments TORC1 repression or activation in response to amino acid (AA) availability.iScience · 2021Article
- Loss of FLCN-FNIP1/2 induces a non-canonical interferon response in human renal tubular epithelial cells.eLife · 2021Article
- Folliculin: A Regulator of Transcription Through AMPK and mTOR Signaling Pathways.Frontiers in cell and developmental biology · 2021Review
- Cryo-EM structure of C9ORF72-SMCR8-WDR41 reveals the role as a GAP for Rab8a and Rab11a.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Nutrient Signaling and Lysosome Positioning Crosstalk Through a Multifunctional Protein, Folliculin.Frontiers in cell and developmental biology · 2020Review
- Article
- Structural mechanism of a Rag GTPase activation checkpoint by the lysosomal folliculin complex.Science (New York, N.Y.) · 2019Article
- GATOR1-dependent recruitment of FLCN-FNIP to lysosomes coordinates Rag GTPase heterodimer nucleotide status in response to amino acids.The Journal of cell biology · 2018Article
- Signal integration in the (m)TORC1 growth pathway.Frontiers in biology · 2018Article
- Review
- Article
- C9orf72: At the intersection of lysosome cell biology and neurodegenerative disease.Traffic (Copenhagen, Denmark) · 2017Review
- Folliculin - A tumor suppressor at the intersection of metabolic signaling and membrane traffic.Small GTPases · 2017Review
- C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling.Molecular biology of the cell · 2016Article
- Folliculin directs the formation of a Rab34-RILP complex to control the nutrient-dependent dynamic distribution of lysosomes.EMBO reports · 2016Article
- FLCN regulates transferrin receptor 1 transport and iron homeostasis.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The folliculin/Fnip complex has been demonstrated to play a crucial role in the mechanisms underlying Birt-Hogg-Dubé (BHD) syndrome, a rare inherited cancer syndrome. Lst4 has been previously proposed to be the Fnip1/2 orthologue in yeast and therefore a member of the DENN family. In order to confirm this, we solved the crystal structure of the N-terminal region of Lst4 from Kluyveromyces lactis and show it contains a longin domain, the first domain of the full DENN module. Furthermore, we demonstrate that Lst4 through its DENN domain interacts with Lst7, the yeast folliculin orthologue. Like its human counterpart, the Lst7/Lst4 complex relocates to the vacuolar membrane in response to nutrient starvation, most notably in carbon starvation. Finally, we express and purify the recombinant Lst7/Lst4 complex and show that it exists as a 1 : 1 heterodimer in solution. This work confirms the membership of Lst4 and the Fnip proteins in the DENN family, and provides a basis for using the Lst7/Lst4 complex to understand the molecular function of folliculin and its role in the pathogenesis of BHD syndrome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.