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Acylation of myelin Po protein is required for adhesion

✍ Scribed by Ying Gao; Wenhui Li; Marie T. Filbin

Publisher: John Wiley and Sons
Year: 2000
Tongue: English
Weight: 230 KB
Volume: 60
Category: Article
ISSN: 0360-4012
DOI: 10.1002/1097-4547(20000615)60:6<704::aid-jnr2>3.0.co;2-5

No coin nor oath required. For personal study only.

✦ Synopsis

The extracellular domains of myelin Po protein interact homophilically and hence hold myelin compact at the intraperiod line. The cytoplasmic domain of Po, however, can also affect the interactions of its extracellular sequences. Po is acylated, mostly with palmitic acid, at Cys 153, just at the transmembrane:cytoplasmic domain interface. Here we show that Po mutated at Cys 153 to alanine (C153A), is not acylated and is not adhesive. Like wild-type Po, C153A Po clusters within the membrane and seems to interact with the cytoskeleton. On the other hand, the rate of turnover of C153A Po in transfected Chinese hamster ovary cells is almost 4 times faster than wild-type Po. The increased instability of C153A Po compared to wild-type Po may account for its loss of adhesion.

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