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Article

Deep mutational scanning reveals a correlation between degradation and toxicity of thousands of aspartoacylase variants.

Nature communications - 13 May 2024

Grønbæk-Thygesen Martin, Voutsinos Vasileios, Johansson Kristoffer E, Schulze Thea K, Cagiada Matteo, Pedersen Line, Clausen Lene, Nariya Snehal, Powell Rachel L, Stein Amelie, Fowler Douglas M, Lindorff-Larsen Kresten, Hartmann-Petersen Rasmus

Abstract excerpt

Unstable proteins are prone to form non-native interactions with other proteins and thereby may become toxic. To mitigate this, destabilized proteins are targeted by the protein quality control network. Here we present systematic studies of the cytosolic aspartoacylase, ASPA, where variants are linked to Canavan disease, a lethal neurological disorder. We determine the abundance of 6152 of the 6260 ( ~ 98%)...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 38740822
DOI: 10.1038/s41467-024-48481-0
PMCID: PMC11091098

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