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Titolo:
Neuronal inwardly rectifying K+ channels differentially couple to PDZ proteins of the PSD-95/SAP90 family
Autore:
Nehring, RB; Wischmeyer, E; Doring, F; Veh, RW; Sheng, M; Karschin, A;
Indirizzi:
Max Planck Inst Biophys Chem, D-37070 Gottingen, Germany Max Planck Inst Biophys Chem Gottingen Germany D-37070 ottingen, Germany Massachusetts Gen Hosp, Howard Hughes Med Inst, Boston, MA 02114 USA Massachusetts Gen Hosp Boston MA USA 02114 Med Inst, Boston, MA 02114 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 1, volume: 20, anno: 2000,
pagine: 156 - 162
SICI:
0270-6474(20000101)20:1<156:NIRKCD>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECTIFIER POTASSIUM CHANNEL; NMDA RECEPTOR SUBUNITS; POSTSYNAPTIC DENSITY; FUNCTIONAL EXPRESSION; RAT-BRAIN; GUANYLATE KINASES; HUMAN HIPPOCAMPUS; MOLECULAR-BASIS; FASCICLIN-II; DOMAIN;
Keywords:
inwardly rectifying; Kir channel; GIRK; postsynaptic density; chapsyns; MAGUK; yeast two-hybrid;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Karschin, A Max Planck Inst Biophys Chem, Fassberg 11, D-37070 Gottingen, Germany Max Planck Inst Biophys Chem Fassberg 11 Gottingen Germany D-37070
Citazione:
R.B. Nehring et al., "Neuronal inwardly rectifying K+ channels differentially couple to PDZ proteins of the PSD-95/SAP90 family", J NEUROSC, 20(1), 2000, pp. 156-162

Abstract

Several signaling proteins clustered at the postsynaptic density specialization in neurons harbor a conserved C-terminal PDZ domain recognition sequence (X-S/T-X-V/I) that mediates binding to members of the PSD-95/SAP90 protein family. This motif is also present in the C termini of some inwardly rectifying K+ (Kir) channels. Constitutively active Kir2 channels as well as G protein-gated Kir3 channels, which are fundamental for neuronal excitability, were analyzed as candidates for binding to PSD-95/SAP90 family members. Therefore C termini of Kir2.1(+), Kir2.3(+), Kir2.4(-), Kir3.1(-), Kir3.2(-), Kir3.3(-) and Kir3.4(-) subunits (+, motif present; -, motif absent) were used as baits in the yeast two-hybrid assay to screen for in vivo interaction with PDZ domains 1-3 of PSD-95/SAP90. In contrast to Kir2.1 and Kir2.3, all Kir3 fragments failed to bind PSD-95 in this assay, which was supported by the lack of coimmunoprecipitation and colocalization of the entire proteins in mammalian cells. A detailed analysis of interaction domains demonstrated that the C-terminal motif in Kir3 channels is insufficient for binding PDZ domains. Kir2.1 and Kir2.3 subunits on the other hand coprecipitate with PSD-95. When coexpressed in a bicistronic internal ribosome entry site expression vector in HEK-293 cells macroscopic and elementary current analysis revealed that PSD-95 suppressed the activity of Kir2.3 channels by >50%. This inhibitory action of PSD-95, which predominantly affects the single-channel conductance, is likely attributable to a molecular association with additional internal interaction sites in the Kir2.3 protein.

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Documento generato il 22/09/20 alle ore 11:24:23