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- W2000272692 abstract "P2Y 1 purinergic receptors (P2Y 1 Rs) mediate rises in intracellular Ca 2+ in response to ATP, but the duration and characteristics of this Ca 2+ response are known to vary markedly in distinct cell types. We screened the P2Y 1 R carboxyl terminus against a recently created proteomic array of PDZ (PSD-95/ Drosophila Discs large/ZO-1 homology) domains and identified a previously unrecognized, specific interaction with the second PDZ domain of the scaffold NHERF-2 (Na + /H + exchanger regulatory factor type 2). Furthermore, we found that P2Y 1 R and NHERF-2 associate in cells, allowing NHERF-2-mediated tethering of P2Y 1 R to key downstream effectors such as phospholipase Cβ. Finally, we found that coexpression of P2Y 1 R with NHERF-2 in glial cells prolongs P2Y 1 R-mediated Ca 2+ signaling, whereas disruption of the P2Y 1 R–NHERF-2 interaction by point mutations attenuates the duration of P2Y 1 R-mediated Ca 2+ responses. These findings reveal that NHERF-2 is a key regulator of the cellular activity of P2Y 1 R and may therefore determine cell-specific differences in P2Y 1 R-mediated signaling." @default.
- W2000272692 created "2016-06-24" @default.
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- W2000272692 date "2005-05-18" @default.
- W2000272692 modified "2023-09-26" @default.
- W2000272692 title "P2Y <sub>1</sub> receptor signaling is controlled by interaction with the PDZ scaffold NHERF-2" @default.
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- W2000272692 doi "https://doi.org/10.1073/pnas.0408818102" @default.
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