Specifically, in the basal state Perilipin A allows a low level of basal lipolysis by reducing the access of cytosolic lipases to stored triacylglycerol in LDs. It is found at their surface in a complex with CGI-58, the co-activator of ATGL. ATGL might also be in this complex but it is quiescent.
Under lipolytically stimulated conditions, PKA is activated and phosphorylates up to 6 Serine residues on Perilipin A (Ser81, 222, 276, 433, 492, and 517) and 2 on HSL (Ser659, and 660). Although PKA also phosphorylates HSL, which can increase its activity, the more than 50-fold increase in fat mobilization (triggered by epinephrine) is primarily due to Perilipin phosphorylation.
Then, Phosphorylated HSL translocates to the LD surface and associates with Perilipin A and Adipocyte fatty acid-binding protein (AFABP). Consequently, HSL gains access to triacylglycerol (TAG) and diacylglycerol (DAG), substrates in LDs. Also, CGI-58 separates from the LD outer layer which leads to a redistribution of ATGL. In particular, ATGL interacts with Perilipin A through phosphorylated Ser517.
As a result, PKA phosphorylation implies an enriched colocation of HLS and ATGL which facilitates maximal lipolysis by the two lipases.