Toxic Peptides Disrupt Membrane-less Organelles in Neurodegenerative Disease
Researchers at St. Jude Children’s Research Hospital have discovered the way toxic proteins linked to the most common forms of amyotrophic lateral sclerosis (ALS) and frontotemproal dementia (FTD) incapacitate membrane-less organelles inside cells. The toxic peptides directly interfere with the assembly and function of these essential compartments by disturbing normal phase transitions, the processes that allow membrane-less organells to assemble and function. The new work builds upon a previous study from St. Jude that was published in 2015. That earlier work revealed how an ALS-causing mutation in an RNA-binding protein (hnRNPA1) disturbed the same phase separation process that leads to impairment of membrane-less organelles. “Our new findings help build a more cohesive picture of the molecular mechanisms for both of these debilitating neurodegenerative diseases,” said J. Paul Taylor, MD, PhD, a Howard Hughes Medical Institute (HHMI) investigator and chair of the St. Jude Department of Cell and Molecular Biology. “Researchers have identified many impaired processes within the cell when these diseases strike, but it has been more challenging to untie these findings into a unified mechanism. Our results help account for the many widespread cellular abnormalities observed in both ALS and FTD and set the stage for future studies to look at new drug interventions.” Click here to read more.
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