Myelin basic protein (MBP) binds to negatively charged lipids on the cytosolic surface of oligodendrocyte membranes and is responsible for adhesion of these surfaces in multilayered Myelin sheaths. As a member of a larger family of proteins with many forms and post-translational modifications, MBP appears to have several other functions as a result of these modifications, including participating in the transmission of extracellular signals, as well as cell signaling. These modifications of MBP are dynamic during normal central nervous system (CNS) development and during Myelin degeneration in multiple sclerosis (MS). Regulation of the human MBP gene occurs at the MB1 regulatory motif located between nucleotides -14 to -50. The MB1 element contains binding sites for both the activator protein MEF-1/Pur?and the repressor protein MYEF2. MYEF2 is a nuclear protein whose expression is developmentally regulated in mouse brain with peak expression occurring at postnatal day 7. Four isoforms of MYEF2 exist due to alternative splicing events.