CB1 cannabinoid receptor-phosphorylated fourth intracellular loop structure-function relationships.

ABSTRACT: A peptide comprising the juxtamembrane C-terminal intracellular loop 4 (IL4) of the CB₁ cannabinoid receptor possesses three Serine residues (Ser402, Ser411 and Ser415). Here we report the effect of Ser phosphorylation on the CB₁ IL4 peptide conformation and cellular signaling functions using nuclear magnetic resonance spectroscopy, circular dichroism, G protein activation and cAMP production. Circular dichroism studies indicated that phosphorylation at various Ser residues induced helical structure in different environments. NMR data indicates that helical content varies in the order of IL4pSer411 > IL4pSer415 > IL4 > IL4pSer402. The efficacy of phosphorylated IL4 peptides in activating Go and Gi3 ([³⁵S]GTPγS binding) and inhibiting cAMP accumulation in N1

SUBMITTER: Eldeeb K 

PROVIDER: S-EPMC7224360 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature