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The study reveals the structure of a lysosomal multienzyme complex (LMC) core, crucial for degrading cellular waste. Understanding these enzyme interactions, like β-galactosidase (GLB1) and protective protein cathepsin A (CTSA), aids in developing therapies for lysosomal storage diseases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Lysosomal enzymes β-galactosidase (GLB1) and neuraminidase 1 (NEU1) degrade glycoproteins and glycolipids.
  • These enzymes require protective protein cathepsin A (CTSA) for stability, forming a lysosomal multienzyme complex (LMC).
  • Defects in GLB1, NEU1, or CTSA cause severe lysosomal storage diseases like GM1-gangliosidosis and sialidosis.

Purpose of the Study:

  • To elucidate the three-dimensional structure of the murine LMC core.
  • To understand the specific interactions between GLB1 and CTSA within the complex.
  • To investigate the impact of mutations on LMC formation and stability.

Main Methods:

  • Determined the high-resolution three-dimensional structure of the murine LMC core.
  • Analyzed the molecular architecture of the 0.8-MDa complex.
  • Investigated the role of the GLB1-CTSA interface through mutation analysis.

Main Results:

  • The murine LMC core features a triangular architecture composed of three GLB1 and three CTSA dimers.
  • A unique polar interface between GLB1 and CTSA is essential for maintaining the complex's structure.
  • Mutations at this interface disrupt LMC formation in vitro, mirroring disease pathology.

Conclusions:

  • The structural insights into the LMC core provide a foundation for understanding lysosomal storage diseases.
  • The identified GLB1-CTSA interface is critical for LMC assembly and function.
  • These findings may guide the development of novel therapeutic strategies for GM1-gangliosidosis, sialidosis, and galactosialidosis.