Protein palmitoylation, the reversible addition of palmitic acid to proteins, is a fundamental cellular mechanism that regulates various ion channels, neurotransmitter receptors, cell adhesion molecules, scaffolding, cytoskeletal and signaling molecules. This lipid modification facilitates vesicular transport and proper subcellular localization of a modified protein to specific plasma membrane domains such as synapses. Consequently, protein palmitoylation is critical for signal transduction, assembly of a protein complex, cell adhesion, neurite outgrowth, synaptic transmission, and plasticity. In mammals, palmitoylation is mediated by 23-24 palmitoyl acyltransferases (PATs), which are also called ZDHHCs because they contain the DHCC domain, a motif composed of aspartate-histidine-histidine-cysteine. Palmitate is removed by depalmitoylation enzymes including palmitoyl thioesterases (PPT1 and 2), acyl palmitoyl transferases (APT1 and 2) and a/ß Hydrolase domain-containing protein 17 (ABHD17A-C). Many of these enzymes and their substrates that regulate palmitoylation and depalmitoylation are associated with various neurological and psychiatric disorders in children and adults. Therefore, this dynamic process is potentially a promising therapeutic target.
The goal of this Research Topic is to collect papers examining the role of protein palmitoylation and depalmitoylation in synaptic plasticity as well as various other stages of neuronal differentiation including neuronal migration, axodendritic polarization, axonal guidance, synapse formation, and myelination. Topic Papers can approach these questions using combinations of genetics, physiology, biochemistry, imaging and in vivo analysis. We welcome any type of contribution including original research, review, and perspective. However, the work should emphasize the significance of palmitoylation.
Protein palmitoylation, the reversible addition of palmitic acid to proteins, is a fundamental cellular mechanism that regulates various ion channels, neurotransmitter receptors, cell adhesion molecules, scaffolding, cytoskeletal and signaling molecules. This lipid modification facilitates vesicular transport and proper subcellular localization of a modified protein to specific plasma membrane domains such as synapses. Consequently, protein palmitoylation is critical for signal transduction, assembly of a protein complex, cell adhesion, neurite outgrowth, synaptic transmission, and plasticity. In mammals, palmitoylation is mediated by 23-24 palmitoyl acyltransferases (PATs), which are also called ZDHHCs because they contain the DHCC domain, a motif composed of aspartate-histidine-histidine-cysteine. Palmitate is removed by depalmitoylation enzymes including palmitoyl thioesterases (PPT1 and 2), acyl palmitoyl transferases (APT1 and 2) and a/ß Hydrolase domain-containing protein 17 (ABHD17A-C). Many of these enzymes and their substrates that regulate palmitoylation and depalmitoylation are associated with various neurological and psychiatric disorders in children and adults. Therefore, this dynamic process is potentially a promising therapeutic target.
The goal of this Research Topic is to collect papers examining the role of protein palmitoylation and depalmitoylation in synaptic plasticity as well as various other stages of neuronal differentiation including neuronal migration, axodendritic polarization, axonal guidance, synapse formation, and myelination. Topic Papers can approach these questions using combinations of genetics, physiology, biochemistry, imaging and in vivo analysis. We welcome any type of contribution including original research, review, and perspective. However, the work should emphasize the significance of palmitoylation.