The Journal of Membrane Biology

, Volume 120, Issue 3, pp 233–246

Major myelin proteolipid: The 4-α-helix topology

  • Jean-Luc Popot
  • Danielle Pham Dinh
  • André Dautigny
Articles

DOI: 10.1007/BF01868534

Cite this article as:
Popot, JL., Dinh, D.P. & Dautigny, A. J. Membrain Biol. (1991) 120: 233. doi:10.1007/BF01868534

Summary

Several conflicting models have been proposed for the membrane arrangement of the major myelin proteolipid (PLP). We have compared features of the sequence of PLP with those of other eukaryotic integral membrane proteins, with the view of identifying the most likely transmembrane topology. A new, simple model is suggested, which features four hydrophobic α-helices spanning the whole thickness of the lipid bilayer. Its orientation may be such that both the N-and C-termini face the cytosol. None of the biochemical, biophysical or immunological experiments hitherto reported provides incontrovertible evidence against the model. The effect or absence thereof of various PLP mutations is discussed in the frame, of the proposed 4-helix topology.

Key Words

PLP DM20 oligodendrocyte myelin sheath Pelizaeus-Merzbacher disease dysmyelination Jimpy mutation integral membrane protein transmembrane topology hydrophobic α-helix hydrophobicity analysis model building prediction 

Copyright information

© Springer-Verlag New York Inc 1991

Authors and Affiliations

  • Jean-Luc Popot
    • 1
  • Danielle Pham Dinh
    • 2
  • André Dautigny
    • 2
  1. 1.Institut de Biologie Physico-Chimique and Collège de FranceC.N.R.S. URA1187ParisFrance
  2. 2.C.N.R.S. URA1188Université Paris 5Paris Cedex 06France

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