Characterization of the effect on adhesion of different mutations in myelin P0 protein.
Table 1 summarizes the results obtained from expressing in CHO cells C21A P0 and N93A P0 alone, and each with wild-type P0. As can be seen, each of these mutated proteins reach the cell surface when expressed alone, but neither is adhesive. Finally, when each of these mutated P0 molecules is expressed with the wild-type P0, wild-type P0 is no longer adhesive. Therefore, both C21A Po and N93A P0 each have a dominant negative effect on adhesion of wild-type P0. This approach to address the functional consequences of mutations in P0 can now be used to assess the effects of different mutations associated with CMT1B.
Filbin
M T
MT
Department of Biological Sciences, Hunter College of CUNY, New York 10021, USA. filbin@genectr.hunter.cuny.edu
Zhang
K
K
Li
W
W
Gao
Y
Y
D019943:Amino Acid Substitution; D000818:Animals; D016466:CHO Cells; D002448:Cell Adhesion / Q000502:physiology*; D006224:Cricetinae; D006801:Humans; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D018993:Myelin P0 Protein / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D017354:Point Mutation; D011487:Protein Conformation; D014162:Transfection
D018993:Myelin P0 Protein