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Background We recently reported that mutation of the cGMP-dependent Protein Kinase G I alpha (PKGIa) N-terminal leucine zipper (LZ) domain (in the PKGIa LZ mutant, or LZM, mouse) accelerates cardiac remodeling and heart failure after left ventricular (LV) pressure overload, and prevents the anti-remodeling effect of sildenafil [1]. We therefore hypothesized that PKGIa attenuates remodeling by regulating cardiac signaling pathways that are dependent on substrate interactions mediated by its LZ domain. As a first step to identifying cardiac proteins downstream of PKGIa, we screened myocardial lysates for PKGIa LZ domain-interacting proteins. Our previous work revealed a requirement for the PKGIa LZ domain for the activation of anti-remodeling myocardial JNK activity after LV pressure overload. MLK3 is a MAPKKK that contains an LZ domain and activates JNK.

Identification of protein kinase G I alpha interacting proteins as potential targets to prevent cardiac remodeling