Neuropathological protein aggregates are a hallmark of ALS pathology and are commonly thought to exert detrimental effects on motor neuron survival. Two disruptive studies, published in Nature Communications and Plos One from Prof. Gerardo Lederkremer and Dr. Julia Leitman of Tel Aviv University’s Department of Cell Research and Immunology, in collaboration with Prof. Ulrich Hartl of the Max Planck Institute for Biochemistry, demonstrate an opposite function for these protein clusters. The researchers found that in both striatal cell lines expressing mutant huntingtin and in the striatum of Huntington’s disease mouse models, striatal neurons are particularly sensitive to endoplasmic reticulum (ER) stress. Mutant huntingtin triggers the ER stress response well before the protein accumulates as protein aggregates. Surprisingly, the protein aggregates appear to exert a protective effect on the stressed striatal neurons. These findings call into question the current therapeutic strategies directed at disrupting protein aggregation, and reveal novel therapeutic targets for attenuating the ER stress response. To read more about these potentially ground-breaking studies, click here.
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