Abstract
Protein zero (P0) is an integral transmembrane glycoprotein that serves as the major protein component of peripheral nerve myelin and is a member of the immunoglobulin (IgG) gene superfamily. As a cell adhesion molecule, P0 mediates homophilic adhesive interactions between Schwann cell plasma membranes and is a key structural constituent of both the major dense line and intraperiod line of compact myelin. Both the extracellular and cytoplasmic domains contribute to these interactions and evidence indicates that the post-translational modifications of the molecule, including glycosylation, acylation and phosphorylation, play an important modulatory role in adhesion and likely in the proper trafficking of P0 from the endoplasmic reticulum to the plasma membrane as well. Structural and genetic studies indicate that mutations in P0 producing human demyelinating diseases probably do so by perturbing or preventing homophilic interactions during myelination, or by producing cellular toxicity or an unstable myelin sheath. A variety of transcription factors, growth factors and neurosteroids both directly and indirectly influence P0 gene expression during maturation of the myelinating Schwann cell. Besides its structural function in myelin, P0 may have roles in the delivery of other Schwann cell proteins to their proper location, especially at or near nodes of Ranvier, and in neuronal-glial interactions.
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Eichberg, J. Myelin P0: New Knowledge and New Roles. Neurochem Res 27, 1331–1340 (2002). https://doi.org/10.1023/A:1021619631869
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DOI: https://doi.org/10.1023/A:1021619631869