Daniela Bertinetti

TL;DR: The main finding is that tetramerization of the C-terminal domain of HCN1 occurs at basal cAMP concentrations, whereas those ofHCN2 and HCN4 require cAMP saturating levels, which underscores that ligand-induced CNBD tetramerized removes tonic inhibition from the pore of HCn channels.

TL;DR: It is clearly demonstrate that LRRK2 kinase activity is modulated by PKA-mediated binding of 14-3-3 to S1444 and suggest that 14- 3-3 interaction with L RRK2 is hampered in R1441C/G/H-mediated PD pathogenesis.

TL;DR: The design of conformationally constrained peptides that disrupt interactions between PKA and AKAPs in an isoform-selective manner are reported, representing a new class of AKAP disruptors to study compartmentalized RII-regulated PKA signaling in cells.

TL;DR: It is reported that the PKG Iβ C-terminal cyclic nucleotide binding domain (CNB-B) is highly selective for cGMP binding, and crystal structures of CNB-B with and without bound cG MP are solved.

TL;DR: It is demonstrated that the chemotaxis protein CheR1 is a methyltransferase that binds S-adenosylmethionine and transfers a methyl group from this methyl donor to the chemoreceptor PctA, an activity which can be stimulated by the attractant serine but not by glutamine.