AKAP6 and phospholamban colocalize and interact in HEK-293T cells and primary murine cardiomyocytes.

ABSTRACT: Phospholamban (PLN) is an important Ca²⁺ modulator at the sarcoplasmic reticulum (SR) of striated muscles. It physically interacts and inhibits sarcoplasmic reticulum Ca²⁺ ATPase (SERCA2) function, whereas a protein kinase A (PKA)-dependent phosphorylation at its serine 16 reverses the inhibition. The underlying mechanism of this post-translational modification, however, remains not fully understood. Using publicly available databases, we identified A-kinase anchoring protein 6 (AKAP6) as a candidate that might play some roles in PLN phosphorylation. Immunofluorescence showed colocalization between GFP-AKAP6 and PLN in transfected HEK-293T cells and cultured mouse neonatal cardiomyocytes (CMNCs). Co-immunoprecipitation confirmed the functional interaction between AKAP

SUBMITTER: Hakem Zadeh F 

PROVIDER: S-EPMC6642276 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature