The tyrosine phosphatase Shp-2 interacts with the dopamine D1 receptor and triggers D1-mediated Erk signaling in striatal neurons
The tyrosine phosphatase Shp-2 interacts with the dopamine D1 receptor and triggers D1-mediated Erk signaling in striatal neurons
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DOI:
10.1111/j.1471-4159.2011.07196.x
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发表时间:
2011-04-01
影响因子:
4.7
通讯作者:
Missale, Cristina
中科院分区:
文献类型:
--
作者:
Fiorentini, Chiara;Mattanza, Cinzia;Missale, Cristina
P>We report a novel mechanism for dopamine D-1 receptor (D1R)-mediated extracellular signal-regulated kinases (Erk) activation in rat striatum. Erk signaling depends on phosphorylation and dephosphorylation events mediated by specific kinases and phosphatases. The tyrosine phosphatase Shp-2, that is required for Erk activation by tyrosine kinase receptors, has been recently shown to regulate signaling downstream of few G protein-coupled receptors. We show that the D1R interacts with Shp-2, that D1R stimulation results in Shp-2 tyrosine phosphorylation and activation in primary striatal neuronal cultures and that D1R/Shp-2 interaction is required for transmitting D1R-dependent signaling to Erk1/2 activation. D1R-mediated Erk1/2 phosphorylation in cultured striatal neurons is in fact abolished by over-expression of the inactive Shp-2(C/S) mutant and by small interfering RNA-induced Shp-2 silencing. Moreover, by using selective inhibitors we show that both D1R-induced Shp-2 activation and Erk1/2 phosphorylation are dependent on the cyclic AMP/protein kinase A pathway and require Src. These results, which were substantiated also in transfected human embryonic kidney 293 cells, provide a novel mechanism by which to converge D1R signaling to the Erk pathway and suggest that Shp-2 or the D1R/Shp-2 interface could represent a potential drug target for disorders of dopamine transmission involving malfunctioning of D1R signaling.