title: Postsynaptic nanodomains generated by local palmitoylation cycles.
abstract: Precise regulation of protein assembly at specialized membrane domains is essential for diverse cellular functions including synaptic transmission. However, it is incompletely understood how protein clustering at the plasma membrane is initiated, maintained and controlled. Protein palmitoylation, a common post-translational modification, regulates protein targeting to the plasma membrane. Such modified proteins are enriched in these specialized membrane domains. In this review, we focus on palmitoylation of PSD-95, which is a major postsynaptic scaffolding protein and makes discrete postsynaptic nanodomains in a palmitoylation-dependent manner and discuss a determinant role of local palmitoylation cycles in creating highly localized hotspots at the membrane where specific proteins concentrate to organize functional domains.
authors: *Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences; and Department of Physiological Sciences, School of Life Science, SOKENDAI (the Graduate University for Advanced Studies), Okazaki 444-8787, Japan.
authors: Masaki
authors: M
authors: Fukata
authors: *Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences; and Department of Physiological Sciences, School of Life Science, SOKENDAI (the Graduate University for Advanced Studies), Okazaki 444-8787, Japan.
authors: Atsushi
authors: A
authors: Sekiya
authors: *Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences; and Department of Physiological Sciences, School of Life Science, SOKENDAI (the Graduate University for Advanced Studies), Okazaki 444-8787, Japan.
authors: Tatsuro
authors: T
authors: Murakami
authors: *Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences; and Department of Physiological Sciences, School of Life Science, SOKENDAI (the Graduate University for Advanced Studies), Okazaki 444-8787, Japan.
authors: Norihiko
authors: N
authors: Yokoi
authors: *Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences; and Department of Physiological Sciences, School of Life Science, SOKENDAI (the Graduate University for Advanced Studies), Okazaki 444-8787, Japan.
authors: Yuko
authors: Y
authors: Fukata
mesh_terms: D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism; D000076122:Disks Large Homolog 4 Protein; D006624:Hippocampus / Q000378:metabolism; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism*; D054878:Lipoylation / Q000235:genetics*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009474:Neurons / Q000378:metabolism; D013569:Synapses / Q000235:genetics / Q000378:metabolism; D009435:Synaptic Transmission / Q000235:genetics*
chemical_list: C501444:DLG4 protein, human; D000076122:Disks Large Homolog 4 Protein; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins