Abstract:
:Protein kinase A (PKA) is a key regulator of neurosecretion, but the molecular targets remain elusive. We combined pharmacological manipulations of kinase and phosphatase activities with mutational studies on the exocytotic machinery driving fusion of catecholamine-containing vesicles from chromaffin cells. We found that constitutive PKA activity was necessary to maintain a large number of vesicles in the release-ready, so-called primed, state, whereas calcineurin (protein phosphatase 2B) activity antagonized this effect. Overexpression of the SNARE protein SNAP-25a mutated in a PKA phosphorylation site (Thr-138) eliminated the effect of PKA inhibitors on the vesicle priming process. Another, unidentified, PKA target regulated the relative size of two different primed vesicle pools that are distinguished by their release kinetics. Overexpression of the SNAP-25b isoform increased the size of both primed vesicle pools by a factor of two, and mutations in the conserved Thr-138 site had similar effects as in the a isoform.
journal_name
Neuronjournal_title
Neuronauthors
Nagy G,Reim K,Matti U,Brose N,Binz T,Rettig J,Neher E,Sørensen JBdoi
10.1016/s0896-6273(04)00038-8subject
Has Abstractpub_date
2004-02-05 00:00:00pages
417-29issue
3eissn
0896-6273issn
1097-4199pii
S0896627304000388journal_volume
41pub_type
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