FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2892425659> ?p ?o ?g. }

• W2892425659 endingPage "17753" @default.
• W2892425659 startingPage "17739" @default.
• W2892425659 abstract "Kir7.1 is an inwardly rectifying potassium channel with important roles in the regulation of the membrane potential in retinal pigment epithelium, uterine smooth muscle, and hypothalamic neurons. Regulation of G protein–coupled inwardly rectifying potassium (GIRK) channels by G protein–coupled receptors (GPCRs) via the G protein βγ subunits has been well characterized. However, how Kir channels are regulated is incompletely understood. We report here that Kir7.1 is also regulated by GPCRs, but through a different mechanism. Using Western blotting analysis, we observed that multiple GPCRs tested caused a striking reduction in the complex glycosylation of Kir7.1. Further, GPCR-mediated reduction of Kir7.1 glycosylation in HEK293T cells did not alter its expression at the cell surface but decreased channel activity. Of note, mutagenesis of the sole Kir7.1 glycosylation site reduced conductance and open probability, as indicated by single-channel recording. Additionally, we report that the L241P mutation of Kir7.1 associated with Lebers congenital amaurosis (LCA), an inherited retinal degenerative disease, has significantly reduced complex glycosylation. Collectively, these results suggest that Kir7.1 channel glycosylation is essential for function, and this activity within cells is suppressed by most GPCRs. The melanocortin-4 receptor (MC4R), a GPCR previously reported to induce ligand-regulated activity of this channel, is the only GPCR tested that does not have this effect on Kir7.1. Kir7.1 is an inwardly rectifying potassium channel with important roles in the regulation of the membrane potential in retinal pigment epithelium, uterine smooth muscle, and hypothalamic neurons. Regulation of G protein–coupled inwardly rectifying potassium (GIRK) channels by G protein–coupled receptors (GPCRs) via the G protein βγ subunits has been well characterized. However, how Kir channels are regulated is incompletely understood. We report here that Kir7.1 is also regulated by GPCRs, but through a different mechanism. Using Western blotting analysis, we observed that multiple GPCRs tested caused a striking reduction in the complex glycosylation of Kir7.1. Further, GPCR-mediated reduction of Kir7.1 glycosylation in HEK293T cells did not alter its expression at the cell surface but decreased channel activity. Of note, mutagenesis of the sole Kir7.1 glycosylation site reduced conductance and open probability, as indicated by single-channel recording. Additionally, we report that the L241P mutation of Kir7.1 associated with Lebers congenital amaurosis (LCA), an inherited retinal degenerative disease, has significantly reduced complex glycosylation. Collectively, these results suggest that Kir7.1 channel glycosylation is essential for function, and this activity within cells is suppressed by most GPCRs. The melanocortin-4 receptor (MC4R), a GPCR previously reported to induce ligand-regulated activity of this channel, is the only GPCR tested that does not have this effect on Kir7.1." @default.
• W2892425659 created "2018-10-05" @default.
• W2892425659 creator A5011382351 @default.
• W2892425659 creator A5022196205 @default.
• W2892425659 creator A5036609969 @default.
• W2892425659 creator A5037511735 @default.
• W2892425659 creator A5052467034 @default.
• W2892425659 creator A5054823377 @default.
• W2892425659 date "2018-11-01" @default.
• W2892425659 modified "2023-10-16" @default.
• W2892425659 title "G protein–coupled receptors differentially regulate glycosylation and activity of the inwardly rectifying potassium channel Kir7.1" @default.
• W2892425659 cites W1900482019 @default.
• W2892425659 cites W1968997865 @default.
• W2892425659 cites W1974853045 @default.
• W2892425659 cites W1979736337 @default.
• W2892425659 cites W1987339646 @default.
• W2892425659 cites W1992149698 @default.
• W2892425659 cites W1992416493 @default.
• W2892425659 cites W2011741529 @default.
• W2892425659 cites W2017310720 @default.
• W2892425659 cites W2022628953 @default.
• W2892425659 cites W2035721067 @default.
• W2892425659 cites W2057657886 @default.
• W2892425659 cites W2070678932 @default.
• W2892425659 cites W2073440103 @default.
• W2892425659 cites W2075864524 @default.
• W2892425659 cites W2076565144 @default.
• W2892425659 cites W2077708836 @default.
• W2892425659 cites W2083971880 @default.
• W2892425659 cites W2090967904 @default.
• W2892425659 cites W2093107542 @default.
• W2892425659 cites W2093986108 @default.
• W2892425659 cites W2098226322 @default.
• W2892425659 cites W2124657728 @default.
• W2892425659 cites W2138098510 @default.
• W2892425659 cites W2145970184 @default.
• W2892425659 cites W2148571014 @default.
• W2892425659 cites W2158375364 @default.
• W2892425659 cites W2161227647 @default.
• W2892425659 cites W2162016919 @default.
• W2892425659 cites W2164256521 @default.
• W2892425659 cites W2337239559 @default.
• W2892425659 cites W2396132292 @default.
• W2892425659 cites W2574882949 @default.
• W2892425659 cites W2575684964 @default.
• W2892425659 cites W2594017777 @default.
• W2892425659 cites W2622196605 @default.
• W2892425659 cites W2802383413 @default.
• W2892425659 cites W2953196813 @default.
• W2892425659 cites W4245814297 @default.
• W2892425659 doi "https://doi.org/10.1074/jbc.ra118.003238" @default.
• W2892425659 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6240878" @default.
• W2892425659 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30257863" @default.
• W2892425659 hasPublicationYear "2018" @default.
• W2892425659 type Work @default.
• W2892425659 sameAs 2892425659 @default.
• W2892425659 citedByCount "13" @default.
• W2892425659 countsByYear W28924256592019 @default.
• W2892425659 countsByYear W28924256592020 @default.
• W2892425659 countsByYear W28924256592021 @default.
• W2892425659 countsByYear W28924256592022 @default.
• W2892425659 countsByYear W28924256592023 @default.
• W2892425659 crossrefType "journal-article" @default.
• W2892425659 hasAuthorship W2892425659A5011382351 @default.
• W2892425659 hasAuthorship W2892425659A5022196205 @default.
• W2892425659 hasAuthorship W2892425659A5036609969 @default.
• W2892425659 hasAuthorship W2892425659A5037511735 @default.
• W2892425659 hasAuthorship W2892425659A5052467034 @default.
• W2892425659 hasAuthorship W2892425659A5054823377 @default.
• W2892425659 hasBestOaLocation W28924256591 @default.
• W2892425659 hasConcept C134018914 @default.
• W2892425659 hasConcept C135285700 @default.
• W2892425659 hasConcept C142652207 @default.
• W2892425659 hasConcept C170493617 @default.
• W2892425659 hasConcept C174510640 @default.
• W2892425659 hasConcept C185592680 @default.
• W2892425659 hasConcept C2777313579 @default.
• W2892425659 hasConcept C50254741 @default.
• W2892425659 hasConcept C55493867 @default.
• W2892425659 hasConcept C62478195 @default.
• W2892425659 hasConcept C80631254 @default.
• W2892425659 hasConcept C83743174 @default.
• W2892425659 hasConcept C86803240 @default.
• W2892425659 hasConcept C94924445 @default.
• W2892425659 hasConcept C95444343 @default.
• W2892425659 hasConceptScore W2892425659C134018914 @default.
• W2892425659 hasConceptScore W2892425659C135285700 @default.
• W2892425659 hasConceptScore W2892425659C142652207 @default.
• W2892425659 hasConceptScore W2892425659C170493617 @default.
• W2892425659 hasConceptScore W2892425659C174510640 @default.
• W2892425659 hasConceptScore W2892425659C185592680 @default.
• W2892425659 hasConceptScore W2892425659C2777313579 @default.
• W2892425659 hasConceptScore W2892425659C50254741 @default.
• W2892425659 hasConceptScore W2892425659C55493867 @default.
• W2892425659 hasConceptScore W2892425659C62478195 @default.
• W2892425659 hasConceptScore W2892425659C80631254 @default.
• W2892425659 hasConceptScore W2892425659C83743174 @default.
• W2892425659 hasConceptScore W2892425659C86803240 @default.

• next