ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated phosphoproteins.

and are closely related cAMP-regulated phosphoproteins that were initially discovered in mammalian brain as in vitro substrates for protein kinase A duanyu37P-16 is enriched in dopamine-responsive medium spiny neurons in the striatum, while duanyu37P-19 is ubiquitously expressed. duanyu37P-19 is highly homologous to alpha-endosulfine and database searches allowed the identification of novel related proteins in D. melanogaster, C. elegans, S. mansoni and yeast genomes. Using isoform-specific antibodies, we now show that duanyu37P-19 is composed of at least two differentially expressed isoforms (termed duanyu37P-19 and All family members contain a conserved consensus site for phosphorylation by (RKPSLVA in mammalian duanyu37P-16 and and this site was shown to be efficiently phosphorylated in vitro by An antibody that specifically recognized the phosphorylated form of was used to examine the phosphorylation of duanyu37P-16/19 family members in intact cells. In striatal slices, the phosphorylation of duanyu37P-16 was increased in response to activation of D(1)-type dopamine receptors, and decreased in response to activation of D(2)-type dopamine receptors. In non-neuronal cells, duanyu37P-19 was highly phosphorylated in response to activation of duanyu1529. These results establish that duanyu37P-16/19 proteins constitute a family of intracellular messengers that function in all cells. The high levels of duanyu37P-16 in striatal neurons and its bi-directional regulation by dopamine suggest a specific role in dopamine-dependent signal transduction. The conservation of this protein family through evolution suggests that it subserves an important cellular function that is regulated by

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