Alternatively Spliced Focal Adhesion Kinase in Rat Brain with Increased Autophosphorylation Activity

International audiencepp125 focal adhesion kinase (FAK), a cytoplasmic tyrosine kinase transducing signals initiated by integrin engagement and G protein-coupled receptors, is highly expressed in brain. FAK from brain had a higher molecular weight and an increased autophosphorylation activity, than from other tissues. In addition to a 9-base insertion in the 3'-coding region, which defines FAK+, rat striatal FAK mRNAs contained several additional short exons, coding for peptides of 28, 6, and 7 residues, respectively (termed boxes 28, 6, and 7), surrounding the autophosphorylated Tyr-397. In transfected COS 7 cells, the presence of boxes 6 and 7 conferred an increased overall tyrosine phosphorylation, a higher phosphorylation of Tyr-397 assessed with a phosphorylation state-specific antibody, and a more active autophosphorylation in immune precipitates. The presence of box 28 did not alter further these parameters. Two-dimensional phosphopeptide maps of hippocampal FAK were identical to those of FAK+6,7. The presence of the various exons did not alter the interaction of FAK with c-Src, n-Src, or Fyn. Thus, several splice isoforms of FAK are preferentially expressed in rat brain, some of which have an increased autophosphorylation activity, suggesting that FAK may have specific properties in neurons

Regulation of a Neuronal Form of Focal Adhesion Kinase by Anandamide

International audienceAnandamide is an endogenous ligand for central cannabinoid receptors and is released after neuronal depolarization. Anandamide increased protein tyrosine phosphorylation in rat hippocampal slices and neurons in culture. The action of anandamide resulted from the inhibition of adenylyl cyclase and cyclic adenosine 3', 5'-monophosphate-dependent protein kinase. One of the proteins phosphorylated in response to anandamide was an isoform of pp125-focal adhesion kinase (FAK+) expressed preferentially in neurons. Focal adhesion kinase is a tyrosine kinase involved in the interactions between the integrins and actin-based cytoskeleton. Thus, anandamide may exert neurotrophic effects and play a role in synaptic plasticity

The Moral Economy of Neoliberalism: How Voters Use Neoliberal Ideology to (De)Legitimate Undocumented Worker Access to Labor Markets

Neoliberalism is prevalent in American life. While researchers have documented the use of neoliberal ideology in institutional and macrolevel policy contexts, they have yet to investigate how voters use neoliberal ideology to legitimate their position on economic policy. I use data from semi-structured interviews with 85 Tucsonans about why they voted the way they did on Proposition 202 (2008): “Arizona Stop Illegal Hiring”— which sought to reregulate undocumented worker labor market access—to address this gap. I found evidence of two distinct neoliberal ideological legitimations: “fair market competition” and “individual responsibility.” Furthermore, I use these data to shed light on the debate over whether neoliberalism spans partisan affiliation or converges with American conservatism. I found that voters across party lines who supported the measure paired neoliberal legitimations with conservative legitimations. We can interpret this bipartisan use of neoliberal ideology as evidence of a neoliberal “moral economy”—or consensus about the moral principles in which market action is embedded. Evidence of this moral economy indicates that moral principles from neoliberal ideology are simultaneously bipartisan and converge with American conservatism. These findings suggest that there could be a broader moral consensus among voters concerning the legitimacy of anti-immigration economic policie