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We hypothesized that secondary molecular changes in PLP<jats:italic><jats:sup>null<\/jats:sup><\/jats:italic>myelin contribute to the loss of PLP\/DM20-dependent neuroprotection and provide more insight into glia-axonal interactions in this disease model. By gel-based proteome analysis, we identified &gt;160 proteins in purified myelin membranes, which allowed us to systematically monitor the CNS myelin proteome of adult PLP<jats:italic><jats:sup>null<\/jats:sup><\/jats:italic>mice, before the onset of disease. We identified three proteins of the septin family to be reduced in abundance, but the nicotinamide adenine dinucleotide (NAD<jats:sup>+<\/jats:sup>)-dependent deacetylase sirtuin 2 (SIRT2) was virtually absent. SIRT2 is expressed throughout the oligodendrocyte lineage, and immunoelectron microscopy revealed its association with myelin. Loss of SIRT2 in PLP<jats:italic><jats:sup>null<\/jats:sup><\/jats:italic>was posttranscriptional, suggesting that PLP\/DM20 is required for its transport into the myelin compartment. Because normal SIRT2 activity is controlled by the NAD<jats:sup>+<\/jats:sup>\/NADH ratio, its function may be coupled to the axo-glial metabolism and the long-term support of axons by oligodendrocytes.<\/jats:p>","DOI":"10.1523\/jneurosci.1254-07.2007","type":"journal-article","created":{"date-parts":[[2007,7,18]],"date-time":"2007-07-18T17:28:28Z","timestamp":1184779708000},"page":"7717-7730","source":"Crossref","is-referenced-by-count":204,"title":["Proteolipid Protein Is Required for Transport of Sirtuin 2 into CNS Myelin"],"prefix":"10.1523","volume":"27","author":[{"given":"Hauke 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