Isoprenoid modification permits 2′,3′-cyclic nucleotide 3′-phosphodiesterase to bind to membranes
✍ Scribed by Dr. P. E. Braun; D. De Angelis; W. W. Shtybel; L. Bernier
- Book ID
- 102912909
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 672 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0360-4012
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✦ Synopsis
The myelination-related enzyme 2' ,3'-cyclic nucleotide 3'-phosphodiesterase (CNP), a relatively abundant protein in the CNS possesses the C-terminal isoprenylation consensus domain found in a small family that includes the rus oncoproteins and their relatives, some G-proteins, and nuclear lamins. We found that CNP, like these other proteins, is modified posttranslationally by an isoprenoid derived from meva-Ionic acid. It appears that only the smaller of the two CNP isoforms (CNP1) is isoprenylated, but similar modification of CNP2 cannot be excluded. Inhibition of isoprenoid synthesis by Lovastatin blocks the binding of newly synthesized CNP to cell membranes; binding is restored upon addition of mevalonate to the culture medium. This shows that isoprenylation is permissive for the well-known avid association of CNP with membranes.
📜 SIMILAR VOLUMES
## Abstract 2′,3′‐Cyclic nucleotide 3′‐phosphodiesterase (CNP) is one of the earliest myelin‐related proteins to be specifically expressed in differentiating oligodendrocytes (ODCs) in the central nervous system (CNS) and is implicated in myelin biogenesis. CNP possesses an in vitro enzymatic activ