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Related Experiment Video

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Author Spotlight: A Selective Luciferase-Based Assay for Monitoring ATG4B 27 Activity in Cells

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Lysosomal ATP Transporter SLC17A9 Controls Cell Viability via Regulating Cathepsin D.

Peng Huang^1,2,3, Qi Cao³, Mengnan Xu³

¹School of Clinical Medicine, Shanghai University of Medicine and Health Sciences, Shanghai 201318, China.

|March 10, 2022

Summary

Solute carrier family 17 member 9 (SLC17A9) deficiency causes cell death via lysosomal dysfunction. Restoring Cathepsin D activity rescues this cell death, highlighting SLC17A9

Keywords:

ATP transporter lysosome solute carrier family 17 member 9 (SLC17A9)vesicular nucleotide transporter (VNUT)

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Solute carrier family 17 member 9 (SLC17A9) transports ATP in lysosomes and secretory vesicles.
SLC17A9 inhibition or silencing results in cell death, but the underlying mechanisms are not fully understood.

Purpose of the Study:

To elucidate the molecular mechanisms by which SLC17A9 deficiency leads to cell death.
To investigate the role of lysosomal function and specific proteases in SLC17A9-mediated cell death.

Main Methods:

Investigated the effect of SLC17A9 deficiency on cell viability and lysosomal function.
Utilized transcription factor EB (TFEB) to assess the link between lysosomal dysfunction and cell death.
Examined the impact of SLC17A9 deficiency on the activity of lysosomal proteases, specifically Cathepsin D and Cathepsin B.
Assessed the rescue effects of heterologous expression of Cathepsin D and Cathepsin B.

Main Results:

Cell death induced by SLC17A9 deficiency was rescued by TFEB, indicating lysosomal dysfunction as a key factor.
SLC17A9 deficiency led to the inhibition of Cathepsin D activity.
Heterologous expression of Cathepsin D successfully rescued lysosomal dysfunction and cell death.
Cathepsin B activity remained unaltered, and its overexpression did not rescue the observed phenotype.

Conclusions:

Lysosomal ATP transport by SLC17A9 is critical for maintaining lysosomal function and cell viability.
SLC17A9 deficiency impairs lysosomal function primarily through the inhibition of Cathepsin D activity.
Targeting Cathepsin D may offer a therapeutic strategy for conditions involving SLC17A9 dysfunction.