Luteinizing hormone (LH) stimulates ovulation, luteal development, and progesterone biosynthesis. Here we summarize recent progress towards understanding cellular and organelle-specific changes induced by LH in steroidogenic luteal cells. LH activates a protein kinase A (PKA)-hormone-sensitive lipase (HSL) signaling pathway. A dynamic relationship has been established among AMP Kinase, PKA, HSL, and lipid droplets (LD) in luteal progesterone synthesis. Analysis of the LD proteome following activation of PKA revealed increased association of active HSD3B with LD. LH via PKA also acutely regulates mitochondrial (Mito) dynamics via phosphorylation of dynamin-related protein 1 (DRP1), decreasing the association of DRP1 with Mito and stimulating Mito fusion. Inhibition of DRP1 of association with Mito elevates LH-induced progesterone biosynthesis. LH induces rapid changes in key metabolic pathways including glycolysis, tricarboxylic acid cycle, pentose phosphate pathway, de novo lipogenesis, and hydrolysis of phospholipids. LH via PKA signaling stimulates phosphorylation of Acetyl-CoA carboxylase (ACACA) and ATP citrate lyase (ACLY), enzymes involved in de novo synthesis of fatty acids. Inhibition of ACLY and fatty acid transport to mitochondria suppresses LH-stimulated progesterone production and phosphorylation of PKA substrates. In summary, LH sensitive and organelle-specific pathways are essential for maintaining signaling and steroidogenesis in ovarian luteal cells.