FAU Researchers Discover Cell Tunnels Spreading Huntington's Disease

New study reveals a pathway that allows toxic proteins to move between brain cells, offering potential treatment target.

Mar. 21, 2026 at 5:04am

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Researchers at Florida Atlantic University have identified a previously unknown cellular pathway that allows brain cells to directly pass toxic proteins responsible for Huntington's disease to their neighbors through tiny, tube-like structures called "tunneling nanotubes." The study shows that disrupting this pathway dramatically reduces the spread of the disease-causing protein in the brain, offering a potential new target for treating Huntington's and other neurodegenerative disorders.

Why it matters

Huntington's disease is a devastating and incurable brain disorder, and understanding how the disease-causing proteins spread between cells is crucial for developing effective treatments. This discovery of a specific cellular mechanism driving that spread provides an exciting new avenue for intervention that could slow or even halt disease progression.

The details

The researchers found that a protein called Rhes, already known to play a key role in Huntington's, partners with a bicarbonate transporter called SLC4A7 to help build the tunneling nanotubes that allow toxic huntingtin proteins to move between neurons. By blocking SLC4A7, either genetically or with drugs, the team was able to prevent the nanotubes from forming and stop the spread of the harmful proteins in mouse models of the disease.

  • The study was published in the journal Science Advances on March 21, 2026.

The players

Srinivasa Subramaniam

Senior author of the study, associate professor in the Department of Chemistry and Biochemistry within FAU's Charles E. Schmidt College of Science, and a member of FAU's Stiles-Nicholson Brain Institute, David and Lynn Nicholson Center for Neuroscience Research, and the Center for Molecular Biology and Biotechnology.

Randy Blakely

Executive director of the FAU Stiles-Nicholson Brain Institute, the David J.S. Nicholson Distinguished Professor in Neuroscience, and a professor of biomedical science in the FAU Charles E. Schmidt College of Medicine.

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What they’re saying

“This work fundamentally changes how we think about disease progression in Huntington's. We've known that neurons somehow pass toxic proteins to one another, but now we can see the machinery that makes that possible. By identifying SLC4A7 as a key partner of Rhes, we've uncovered a new and potentially druggable target to stop that spread at its source.”

— Srinivasa Subramaniam, Senior author, associate professor

“This research shines a spotlight on an entirely new way cells communicate in health and disease. By learning how harmful proteins physically move from cell to cell, we gain powerful new leverage points for therapy. The idea that we could slow or even halt disease progression by blocking these microscopic tunnels opens an exciting frontier for treating not only Huntington's disease, but a wide range of neurological disorders and cancers in the future.”

— Randy Blakely, Executive director, FAU Stiles-Nicholson Brain Institute

What’s next

The researchers plan to continue exploring ways to pharmacologically target the SLC4A7 protein and disrupt the tunneling nanotube pathway as a potential treatment for Huntington's disease and other neurodegenerative disorders.

The takeaway

This breakthrough discovery of a specific cellular mechanism driving the spread of toxic proteins in Huntington's disease opens up an exciting new avenue for developing therapies that could slow or even halt the progression of this devastating disorder, as well as other neurodegenerative diseases and cancers that involve similar intercellular communication pathways.