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Acylation of myelin Po protein is required for adhesion
Author(s) -
Gao Ying,
Li Wenhui,
Filbin Marie T.
Publication year - 2000
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/1097-4547(20000615)60:6<704::aid-jnr2>3.0.co;2-5
Subject(s) - chinese hamster ovary cell , extracellular , chemistry , cytoplasm , myelin , wild type , transmembrane protein , transmembrane domain , acylation , l1 , biochemistry , microbiology and biotechnology , biophysics , biology , amino acid , mutant , gene , receptor , neuroscience , catalysis , central nervous system
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. J. Neurosci. Res. 60:704–713, 2000. © 2000 Wiley‐Liss, Inc.