Cell-type resolved protein atlas of brain lysosomes identifies SLC45A1-associated disease as a lysosomal disorder

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Authors: Ali Ghoochani, Julia C. Heiby, Eshaan S. Rawat, Uche N. Medoh, Domenico Di Fraia, Wentao Dong, Marc Gastou, Mohit Rastogi, Vincent Hernandez, Kwamina Nyame, Nouf N. Laqtom, William Durso
+8 more Christina Valkova, Alina Isakova, Christoph Kaether, Marius Wernig, Natalia Gomez-Ospina, Christian Franke, Alessandro Ori, Abu-Remaileh Monther
Cited by: 8
References: 107

Abstract

Mutations in lysosomal genes cause neurodegeneration and neuronopathic lysosomal storage disorders (LSDs). Despite their essential role in brain homeostasis, the cell-type-specific composition and function of lysosomes remain poorly understood. Here, we report a quantitative protein atlas of lysosomes from mouse neurons, astrocytes, oligodendrocytes, and microglia. We identify dozens of proteins not previously annotated as lysosomal and reveal the diversity of lysosomal composition across brain cell types. Notably, we identified SLC45A1, a gene whose mutations cause a monogenic neurological disease, as a neuron-specific lysosomal protein. Loss of SLC45A1 causes lysosomal dysfunction in vitro and in vivo. SLC45A1 functions as a lysosomal sugar transporter and impacts the stability of the V1 subunits of the vacuolar ATPase (V-ATPase). Consistently, SLC45A1 loss reduces lysosomal V1 subunits, elevates lysosomal pH, and disrupts iron homeostasis, causing mitochondrial dysfunction. Altogether, our work redefines SLC45A1-associated disease as an LSD and establishes a comprehensive map to study lysosome biology at cell-type resolution.

Fields of Study & Subjects

Lysosomal Storage Disorders Research Calcium signaling and nucleotide metabolism Autophagy in Disease and Therapy

Publication details

Journal / source
Cell
Publisher
Elsevier BV
Volume
189
Issue
3
Pages
765–782.e31
Publication date
22 January 2026
Language
EN