The myelin regulatory factor gene (MYRF) encodes a protein evolutionarily conserved from invertebrates to vertebrates,representing a novel type of membrane-bound transcriptional factor (MBTF).In vertebrates,MYRF protein is required for myelin development and mainte-nance [1,2].Unlike other oligodendrocyte-specific tran-scription factors,it is initially synthesized as a conserved type-II membrane protein,containing a N-terminal proline-rich (Pro) domain,a putative yeast Ndt80-1ike DNA binding domain (DBD),two nuclear localization signal motifs,an intramolecular chaperone auto-processing (ICA)domain,a transmembrane domain,and a function-unknown C-terminal conserved (C) domain (Fig 1).Among these conserved domains,the DBD directly binds to the pro-moters of target genes,the transmembrane domain anchors MYRF to the endoplasmic reticulum (ER) membrane,and the ICA domain drives the homo-trimerization of MYRF protein and subsequently induces its self-cleavage via its intrinsic peptidase activity [3,4].