Proteolipid protein (PLP) is the most abundant protein of central nerv
ous system (CNS) myelin. Because of its predicted topography, PLP has
been assumed to function as a structural component of myelin, providin
g stability and maintaining the compact lamellar structure. However, d
evelopmental studies have shown that the PLP gene is active long befor
e myelination begins, This and other evidence from various PLP mutants
and transgenic models has fueled speculation that PLP or other produc
ts of the gene have additional, nonstructural roles both within and ou
tside the CNS. PLP is structurally related to a family of ion channel
proteins which includes the connexins, synaptophysins and various neur
otransmitter receptors, and there is some experimental evidence which
supports a role for PLP in ion gating, Other provocative ideas are tha
t the PLP gene may influence autocrine signaling within oligodendrocyt
es or that PLP mRNAs have a function apart from protein coding.