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Lysosomal LRRC8 complex impacts lysosomal pH, morphology, and systemic glucose metabolism
Journal article   Open access   Peer reviewed

Lysosomal LRRC8 complex impacts lysosomal pH, morphology, and systemic glucose metabolism

Ashutosh Kumar, Yonghui Zhao, Litao Xie, Rahul Chadda, John D Tranter, Ryan T Mikami, Nihil Abraham, Juan Hong, Ethan Feng, David R Rawnsley, …
Science advances, Vol.11(39), eadt6366
09/26/2025
DOI: 10.1126/sciadv.adt6366
PMCID: PMC12466849
PMID: 41004571
url
https://doi.org/10.1126/sciadv.adt6366View
Published (Version of record) Open Access

Abstract

The lysosome integrates anabolic signaling and nutrient sensing to regulate intracellular growth pathways. The leucine-rich repeat-containing 8 (LRRC8) channel complex forms a lysosomal anion channel and regulates PI3K-AKT-mTOR signaling, skeletal muscle differentiation, growth, and systemic glucose metabolism. Here, we define the endogenous LRRC8 subunits localized to a subset of lysosomes in differentiated myotubes. We show that LRRC8A affects leucine-stimulated mTOR; lysosome size; number; pH; expression of lysosomal proteins LAMP2, P62, and LC3B; and lysosomal function. Mutating an LRRC8A lysosomal targeting dileucine motif sequence (LRRC8A-L706A;L707A) in myotubes recapitulates the abnormal AKT signaling and altered lysosomal morphology and pH observed in LRRC8A knockout cells. In vivo, LRRC8A-L706A;L707A knock-in mice exhibit increased adiposity, impaired glucose tolerance and insulin resistance associated with reduced skeletal muscle PI3K-AKT-mTOR signaling, glucose uptake, and impaired incorporation of glucose into glycogen. These data reveal a lysosomal LRRC8-mediated metabolic signaling function regulating lysosomal function, systemic glucose homeostasis, and insulin sensitivity.
Signal Transduction Animals Glucose - metabolism Humans Hydrogen-Ion Concentration Insulin Resistance Lysosomes - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Mice Mice, Knockout Muscle Fibers, Skeletal - metabolism Muscle, Skeletal - metabolism Phosphatidylinositol 3-Kinases - metabolism Proto-Oncogene Proteins c-akt - metabolism TOR Serine-Threonine Kinases - metabolism

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