@entity935 D2 receptors are involved in the regulation of XXXX and metabotropic @entity3264 receptor 5 phosphorylation in the @entity35 striatum in vivo.

@entity12174 @entity3264 @entity935 @entity10092 @entity35 @entity67415 @entity4149 @entity16497
UNASSIGNED: @entity67415 , a major @entity16497 family kinase (SFK) member that is densely expressed in striatal neurons, is actively involved in the regulation of cellular and synaptic activities in local neurons. This SFK member is likely regulated by @entity935 signaling through a receptor mechanism involving @entity935 D2 receptors (D2Rs). This study characterizes the D2R-dependent regulation of @entity67415 in the @entity35 striatum in vivo. Moreover, we explore whether D2Rs regulate metabotropic @entity3264 receptor 5 ( @entity10092 ) in its @entity4149 phosphorylation and whether the D2R-SFK pathway modulates trafficking of @entity10092 . We found that blockade of D2Rs by systemic administration of a D2R antagonist, @entity12174 , substantially increased SFK phosphorylation in the striatum. This increase was a transient and reversible event. The @entity12174 -induced SFK phosphorylation occurred predominantly in immunopurified @entity67415 but not in another SFK member, @entity16497 . @entity12174 also elevated @entity4149 phosphorylation of @entity10092 . In parallel, @entity12174 enhanced synaptic delivery of active @entity67415 and @entity10092 . Pretreatment with an SFK inhibitor blocked the @entity12174 -induced @entity4149 phosphorylation and synaptic trafficking of @entity10092 . These results indicate that D2Rs inhibit SFK (mainly @entity67415 ) phosphorylation in the striatum. D2Rs also inhibit @entity4149 phosphorylation and synaptic recruitment of @entity10092 through a signaling mechanism likely involving @entity67415 .    2016 Wiley Periodicals, Inc.
