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Isoprenylation of brain 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase modulates cell morphology
Author(s) -
De Angelis D. A.,
Braun P. E.
Publication year - 1994
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/jnr.490390405
Subject(s) - prenylation , microbiology and biotechnology , transfection , cyclic nucleotide phosphodiesterase , phosphodiesterase , cytoplasm , mutant , biology , chemistry , biochemistry , gene , enzyme
CNP (2′,3′‐cyclic nucleotide 3′‐phosphodiesterase) is the earliest myelination specific polypeptide to be synthesized by oligodendrocytes (OLs). When non‐myelinating “naive” cells are transfected with the rat CNP cDNA, CNP accumulates intracellularly in a punctate manner, as well as at the plasma membrane. Filopodia and processes, like those of OLs become elongated and more numerous, and are filled with this protein. Post‐translational isoprenylation of the terminal C‐T‐I‐I sequence with either farnesyl or geranylgeranyl is essential for this phenomenon. In contrast, the non‐isoprenylated C397S mutant is homogeneously distributed throughout the cytoplasm and does not markedly affect cellular morphology. We have sythesized CNP and the C397S mutant in vitro and have shown that isoprenylation is essential for the binding of newly synthesized CNP to myelin. © 1994 Wiley‐Liss, Inc.