SummaryMale germ cells undergo different processes within the female reproductive tract to successfully fertilize the oocyte. These processes are triggered by different extracellular stimuli leading to activation of protein phosphorylation. Protein kinase C (PKC) is a key regulatory enzyme in signal transduction mechanisms involved in many cellular processes. Studies in boar sperm demonstrated a role forPKCin the intracellular signaling involved in motility and cellular volume regulation. Experiments using phorbol 12‐myristate 13‐acetate (PMA) showed increases in the Serine/Threonine phosphorylation of substrates downstream ofPKCin boar sperm. In order to gain knowledge about those cellular processes regulated byPKC, we evaluate the effects ofPMAon boar sperm motility, lipid organization of plasma membrane, integrity of acrosome membrane and sperm agglutination. Also, we investigate the crosstalk betweenPKAandPKCintracellular pathways in spermatozoa from this species. The results presented here reveal a participation ofPKCin sperm motility regulation and membrane fluidity changes, which is probably associated to acrosome reaction and to agglutination. Also, we show the existence of a hierarchy in the kinases pathway. Previous works on boar sperm suggest a pathway in whichPKAis positioned upstream toPKCand this new results support such model.