PRKACA and breast cancer: In addition, MORC2 was phosphorylated at T582 by protein kinase cAMP-activated catalytic subunit alpha (PRKACA), which is activated by G protein-coupled estrogen receptor 1 (GPER1), enhancing its stability by reducing interaction with heat shock protein family A (Hsp70) member 8 (HSPA8) and lysosome-associated membrane protein 2 (LAMP2A), suggesting that phosphorylation modification of MORC2 plays a role in preventing its degradation by chaperone-mediated autophagy (CMA) lysosomes, thereby resulting in E2-mediated BC cell proliferation via the GPER1-PRKACA-MORC2 pathway.28