Analysis of Synaptic Palmitoylated Proteins in a CLN1 Mouse Model
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ABSTRACT: Palmitoylation is a lipid modification that is critical for protein trafficking. Conversely, depalmitoylation detaches palmitic acid from modified proteins in the cytosol or endolysosome to regulate their recycling and degradation. The balance between these two opposing mechanisms controls proteostasis. While the role of palmitoylation is well-established in neuronal differentiation and synaptic plasticity, depalmitoylation is far less understood. Here, we study a lysosomal depalmitoylating enzyme, palmitoyl-protein thioesterase 1 (PPT1), which is associated with the devastating neurodegenerative disease infantile neuronal ceroid lipofuscinosis (CLN1).
INSTRUMENT(S): Q Exactive
ORGANISM(S): Mus Musculus (ncbitaxon:10090)
SUBMITTER: Akira Yoshii Stephanie Cologna
PROVIDER: MSV000094112 | MassIVE | Sun Feb 18 14:57:00 GMT 2024
REPOSITORIES: MassIVE
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