Trimeric G proteins modulate the dynamic interaction of PKAII with the Golgi complex

• DOI: 10.1242/jcs.112.22.3869
• Publication Date: 2021-04-25T17:27:24Z
• Authors: María Esther Martín; Josefina Hidalgo; Francisco M. Vega; Angel Velasco
• Keywords: Brefeldin A; ADP ribosylation factor; Golgi membrane; Transport protein

ABSTRACT The Golgi complex represents a major subcellular location of protein kinase A (PKA) concentration in mammalian cells where it has been previously shown to be involved vesicle-mediated transport processes. We have studied the factors that influence interaction PKA typeII subunits with complex. In addition cytosol, both catalytic (Cα) and regulatory (RIIα) PKAII were detected at sides stack, particularly elements cis- trans-Golgi networks. subunits, contrast, practically absent from middle cisternae. Cell treatment either brefeldin A, AlF4- or low temperature induced dissociation redistribution cytosol. This suggested existence cycle association/dissociation holoenzyme Golgi. purified RIIα membranes was vitro found not affected by while sensitive modulators heterotrimeric G proteins such as AlF4-, GTPγS, βγ mastoparan. binding stimulated recombinant, myristoylated Gαi3 subunit inhibited cAMP. Pretreatment bacterial toxins known catalyze ADP-ribosylation selected Gα also modified binding. Taken together data support role for Golgi-associated recruitment