For decades, the field focused on the plaques and tangles of misfolded proteins that show up in the brains of patients with Alzheimer’s, Parkinson’s and other disorders. The natural assumption was that if you could design a drug to clear out that gunk, you could save the brain. But so far, that bet hasn't paid off.

Now, researchers are taking a big step back and asking whether the plaques aren't a culprit, but rather a clue pointing to something more fundamental going wrong in our brain cells as we age? Put another way, why do our brains get jammed up with these junk proteins in the first place?

Today’s guest, chemical engineer and geneticist Monther Abu-Remaileh, is one of the researchers working hard to answer that question. His research goes deep on a tiny cellular structure called the lysosome, little sacs filled with acid and enzymes that break down worn-out proteins and cellular debris. The lysosome is like a sustainable recycling center for a major city, managing waste streams, recycling raw materials, and coordinating with the rest of the cell to keep things running – and when it breaks down, the whole cell starts to fail. 

Among other accomplishments, Abu-Remaileh, a member of the Knight Initiative for Brain Resilience Steering Committee, has developed clever techniques for probing the lysosome that have put him at the frontier of a transformation in how we think about the lysosome, a transformation that could point the way to slow all manner of neurodegeneration – or even prevent it from happening in the first place.

Learn More

• From humble beginnings to unlocking lysosomal secrets (ASBMB Today, 2026)
• ‘You can literally lose who you are’ (Stanford Report, 2025)
• Driver of neurodegenerative diseases revealed (Stanford Engineering, 2023)
• New atlas could help researchers studying neurological disease (Knight Initiative for Brain Resilience, 2026)
• Sifting through cellular recycling centers (Stanford Engineering, 2022)
• Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes(Science, 2017)
• CLN3 is required for the clearance of glycerophosphodiesters from lysosomes (Nature, 2022)
• The Batten disease gene product CLN5 is the lysosomal bis(monoacylglycero)phosphate synthase (Science, 2023)
• The Bis(monoacylglycero)-phosphate Hypothesis: From Lysosomal Function to Therapeutic Avenues (Annual Review of Biochemistry, 2024)
• PLA2G15 is a BMP hydrolase and its targeting ameliorates lysosomal disease (Nature, 2025)
• Cell-type resolved protein atlas of brain lysosomes identifies SLC45A1-associated disease as a lysosomal disorder(Cell, 2026)

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