Redefining the lipophilin family of proteolipid proteins.
The past few years have seen a dramatic increase in our understanding, in molecular terms, of the involvement of the central nervous system proteolipid protein in myelinogenesis and X-linked genetic diseases. In addition, we have expanded our knowledge of the proteins that have been recruited into the vertebrate myelin membrane over the past 400 million years with the molecular cloning of several cDNAs encoding proteins which are homologous to the proteolipid protein gene. In searching for a name to distinguish these proteins from other "proteolipid" proteins of nonneural origin I propose that we resurrect the term "lipophilins" which describes a small family of unusually hydrophobic integral membrane proteins exhibiting identical topologies and similar physical properties. Two subgroups are distinguishable among the lipophilins based on the patterns of expression during development and the presence or absence of a small motif that is exposed to the extracellular space.
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Brookdale Center for Developmental and Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029-6574, USA. ag4@doc.mssm.edu
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009185:Myelin Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D010802:Phylogeny; D011487:Protein Conformation; D011510:Proteolipids / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D060765:Secretoglobins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014598:Uteroglobin; D014714:Vertebrates
D009185:Myelin Proteins; D011510:Proteolipids; D060765:Secretoglobins; D014598:Uteroglobin