Matt Lucas, Kim Karam, Chowdhury Dhrubajyoti, Hell Johannes W
Department of Pharmacology, Toxicology and Clinical Pharmacy, Institute of Pharmacy, University of Tübingen, Tübingen, Germany.
Department of Pharmacology, University of California, Davis, Davis, CA, United States.
Front Mol Neurosci. 2019 Jan 31;12:8. doi: 10.3389/fnmol.2019.00008. eCollection 2019.
Many postsynaptic proteins undergo palmitoylation, the reversible attachment of the fatty acid palmitate to cysteine residues, which influences trafficking, localization, and protein interaction dynamics. Both palmitoylation by palmitoyl acyl transferases (PAT) and depalmitoylation by palmitoyl-protein thioesterases (PPT) is regulated in an activity-dependent, localized fashion. Recently, palmitoylation has received attention for its pivotal contribution to various forms of synaptic plasticity, the dynamic modulation of synaptic strength in response to neuronal activity. For instance, palmitoylation and depalmitoylation of the central postsynaptic scaffold protein postsynaptic density-95 (PSD-95) is important for synaptic plasticity. Here, we provide a comprehensive review of studies linking palmitoylation of postsynaptic proteins to synaptic plasticity.
许多突触后蛋白会发生棕榈酰化，即脂肪酸棕榈酸酯可逆地附着于半胱氨酸残基上，这会影响蛋白的运输、定位及蛋白相互作用动态。由棕榈酰酰基转移酶（PAT）催化的棕榈酰化和由棕榈酰蛋白硫酯酶（PPT）催化的去棕榈酰化均以活动依赖的局部方式受到调控。最近，棕榈酰化因其对各种形式的突触可塑性（即突触强度对神经元活动的动态调节）的关键作用而受到关注。例如，中枢突触后支架蛋白突触后致密物95（PSD-95）的棕榈酰化和去棕榈酰化对突触可塑性很重要。在此，我们全面综述了将突触后蛋白棕榈酰化与突触可塑性联系起来的研究。
