title: PLPP/CIN regulates bidirectional synaptic plasticity via GluN2A interaction with postsynaptic proteins.
abstract: Dendritic spines are dynamic structures whose efficacies and morphologies are modulated by activity-dependent synaptic plasticity. The actin cytoskeleton plays an important role in stabilization and structural modification of spines. However, the regulatory mechanism by which it alters the plasticity threshold remains elusive. Here, we demonstrate the role of pyridoxal-5'-phosphate phosphatase/chronophin (PLPP/CIN), one of the cofilin-mediated F-actin regulators, in modulating synaptic plasticity in vivo. PLPP/CIN transgenic (Tg) mice had immature spines with small heads, while PLPP/CIN knockout (KO) mice had gigantic spines. Furthermore, PLPP/CIN Tg mice exhibited enhanced synaptic plasticity, but KO mice showed abnormal synaptic plasticity. The PLPP/CIN-induced alterations in synaptic plasticity were consistent with the acquisition and the recall capacity of spatial learning. PLPP/CIN also enhanced N-methyl-D-aspartate receptor (GluN) functionality by regulating the coupling of GluN2A with interacting proteins, particularly postsynaptic density-95 (PSD95). Therefore, these results suggest that PLPP/CIN may be an important factor for regulating the plasticity threshold.
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Ji-Eun
authors.initials: JE
authors.lastname: Kim
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Yeon-Joo
authors.initials: YJ
authors.lastname: Kim
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Duk-Shin
authors.initials: DS
authors.lastname: Lee
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Ji Yang
authors.initials: JY
authors.lastname: Kim
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Ah-Reum
authors.initials: AR
authors.lastname: Ko
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Hye-Won
authors.initials: HW
authors.lastname: Hyun
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Min Ju
authors.initials: MJ
authors.lastname: Kim
authors.affiliation: Department of Anatomy and Neurobiology, Institute of Epilepsy Research, College of Medicine, Hallym University, Chuncheon 200-702, South Korea.
authors.forename: Tae-Cheon
authors.initials: TC
authors.lastname: Kang
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D049229:Dendritic Spines / Q000378:metabolism / Q000473:pathology / Q000502:physiology*; D000076122:Disks Large Homolog 4 Protein / Q000378:metabolism*; D051379:Mice; D018345:Mice, Knockout; D008822:Mice, Transgenic; D009473:Neuronal Plasticity; D010749:Phosphoprotein Phosphatases; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics* / Q000378:metabolism*; D011485:Protein Binding; D016194:Receptors, N-Methyl-D-Aspartate / Q000378:metabolism*; D065852:Spatial Memory
chemical_list: D000199:Actins; D000076122:Disks Large Homolog 4 Protein; D010749:Phosphoprotein Phosphatases; D010744:Phosphoric Monoester Hydrolases; D016194:Receptors, N-Methyl-D-Aspartate; C501447:Dlg4 protein, mouse; C587629:Pdxp protein, mouse