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2’,3’-Cyclic Nucleotide 3’-Phosphodiesterase is a myelin-associated enzyme that makes up 4% of total CNS myelin protein, and is thought to undergo significant age-associated changes.¹ It is named for its ability to catalyze the phosphodiester hydrolysis of 2',3'-cyclic nucleotides to 2'-nucleotides, though a cohesive understanding of its specific physiologic functions are still ambiguous.²

Structural studies have revealed that four classes of CNPs belong to one protein superfamily. CNP's catalytic core consists of three alpha-helices and nine beta-strands. The proposed mechanism of CNPs phosphodiesterase catalytic activity is similar to the second step of the reaction mechanism for RNase A.³

CNP is expressed exclusively by oligodendrocytes in the CNS, and the appearance of CNP seems to be one of the earliest events of oligodendrocyte differentiation.⁴ CNP is thought to play a critical role in the events leading up to myelination.⁵

CNP also associates with microtubules in brain tissue and FRTL-5 thyroid cells, and is reported to have Microtubule-associated protein-like activity (MAP; see MAP2), being able to catalyze microtubule formation at low molar ratios. Deletion of the C-terminus of CNP or phosphorylation abolish the catalytic activity of microtubule formation. CNP can link tubulin to cellular membranes, and might be involved in the regulation cytoplasmic microtubule distribution.⁶

External links

• NCBI Protein

References

1. ^ Hinman, Jason D; Ci-Di Chen, Sun-Young Oh, William Hollander, Carmela R Abraham (2008-01-01). "Age-dependent accumulation of ubiquitinated 2',3'-cyclic nucleotide 3'-phosphodiesterase in myelin lipid rafts". Glia 56 (1): 118-33. ISSN 08941491. 
2. ^ Kursula, P (2008-02). "Structural properties of proteins specific to the myelin sheath". Amino acids 34 (2): 175-85. ISSN 14382199. 
3. ^ Sakamoto, Yasumitsu; Nobutada Tanaka, Tomomi Ichimiya, Tadashi Kurihara, Kazuo T. Nakamura (2005-02-25). "Crystal Structure of the Catalytic Fragment of Human Brain 2',3'-Cyclic-nucleotide 3'-Phosphodiesterase". Journal of Molecular Biology 346 (3): 789-800. doi:10.1016/j.jmb.2004.12.024, http://www.sciencedirect.com/science/article/B6WK7-4F3NVYN-2/1/6c6f243346e6740b69de7883a8d727bd. Retrieved on 14 May 2008. 
4. ^ Kasama-Yoshida, H; Y Tohyama, T Kurihara, M Sakuma, H Kojima, Y Tamai (1997-10). "A comparative study of 2',3'-cyclic-nucleotide 3'-phosphodiesterase in vertebrates: cDNA cloning and amino acid sequences for chicken and bullfrog enzymes". Journal of neurochemistry 69 (4): 1335-42. ISSN 00223042. 
5. ^ Gravel, Michel; John Peterson, Voon Wee Yong, Vicky Kottis, Bruce Trapp, Peter E. Braun (1996-06). "Overexpression of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase in Transgenic Mice Alters Oligodendrocyte Development and Produces Aberrant Myelination". Molecular and Cellular Neuroscience 7 (6): 453-466. doi:10.1006/mcne.1996.0033, http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WNB-45MGT9S-3&_user=10&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=7e45e24639a8728bd180405ac2875e25. Retrieved on 11 May 2008. 
6. ^ Bifulco, Maurizio; Chiara Laezza, Stefania Stingo, J. Wolff (2002-02-19). "2',3'-Cyclic nucleotide 3'-phosphodiesterase: A membrane-bound, microtubule-associated protein and membrane anchor for tubulin". Proceedings of the National Academy of Sciences 99 (4): 1807-1812. doi:10.1073/pnas.042678799, http://www.pnas.org/cgi/content/abstract/99/4/1807. Retrieved on 11 May 2008. 

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