The Myristoylated Alanine Rich C-Kinase Substrate (MARCKS) is a ubiquitous, highly conserved protein among vertebrates, which is essential for postnatal survival, and has been widely studied for its functions in the brain and nervous system. Being highly expressed in nervous tissue, particularly during early development but persisting in the adult, it plays numerous roles related to brain growth, neuronal migration, neurite outgrowth, neurotransmitter release, and synaptic plasticity. Protein kinase C (PKC) phosphorylates MARCKS, which converts MARCKS from a membrane-bound protein to a cytoplasmic protein. The phosphorylation site of MARCKS protein is called the effector domain (ED). Its structure is highly conserved. It can be combined with cell membrane, PKC, calcium/calmodulin-dependent kineses (CaMK) and F-actin. Studies have shown that increased membrane-bound, non-phosphorylated MARCKS might be conducive to the stabilization of synaptic morphology. Phosphorylated MARCKS protein (P-MARCKS) can regulate the stability of actin network and alter the synaptic structure. (PMID: 30655546, PMID: 30155805)