Subcellular compartmentalization of the glycolytic enzyme PFKM regulates cell fate and metabolic switch during skeletal muscle differentiation.

Nature Metabolism, Published online: 24 February 2026; doi:10.1038/s42255-026-01457-4Subcellular compartmentalization of the glycolytic enzyme PFKM regulates cell fate and metabolic switch during skeletal muscle differentiation.

Subcellular compartmentalization of the glycolytic enzyme PFKM regulates cell fate and metabolic switch during skeletal muscle differentiation.

Coenzyme A (CoA), derived from Vitamin B5 (VB5), is essential for lipid metabolism, energy production, and cell proliferation. While the intracellular functions of CoA are well characterized, its tiss...

Petropoulos and colleagues perform single-cell transcriptomics, spatial, functional and comparative analyses, and show that the guinea pig presents high similarity with early human embryogenesis.

Breakdown of every transmembrane protein trafficked to lysosomes requires proteolysis of their hydrophobic helical transmembrane domains. Combining lysosomal proteomics with functional genomic dataset...

A nanoflow multiomic workflow reveals how lysosomal dysfunction disrupts autophagy and mitochondrial homeostasis in LSD mutants.

Bipolar membranes are increasingly being applied in a variety of electrochemical devices, yet understanding of how they operate in complex electrolyte environments is still limited. Here the authors o...

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Development of a targeted protein degradation platform, methylarginine targeting chimera (MrTAC), enables arginine methylation-driven degradation of intracellular proteins in lysosomes.

Pharmaceutical companies are investing in therapies that target proteins for degradation, with trials ongoing for cancer, autoimmune diseases and neurological disorders.

Intracellular DNA assembly for mRNA vaccine compartmentalization facilitates antigen expression and enhances adjuvant efficacy.