2’,3’-Cyclic Nucleotide 3’-Phosphodiesterase


2’,3’-Cyclic Nucleotide 3’-Phosphodiesterase

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GNF_Protein_box
Name = 2',3'-cyclic nucleotide 3' phosphodiesterase


image_source =
PDB = PDB2|1WOJ
HGNCid =
MGIid =
Symbol = CNP
AltSymbols = CNP1
OMIM = 123830
ECnumber =
Homologene = 7672
GeneAtlas_

Function =
Orthologs =

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. [Cite journal
issn = 08941491
volume = 56
issue = 1
pages = 118-33
last = Hinman
first = Jason D
coauthors = Ci-Di Chen, Sun-Young Oh, William Hollander, Carmela R Abraham
title = Age-dependent accumulation of ubiquitinated 2',3'-cyclic nucleotide 3'-phosphodiesterase in myelin lipid rafts
journal = Glia
date = 2008-01-01
] 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. [Cite journal
issn = 14382199
volume = 34
issue = 2
pages = 175-85
last = Kursula
first = P
title = Structural properties of proteins specific to the myelin sheath
journal = Amino acids
date = 2008-02
]

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. [Cite journal
doi = 10.1016/j.jmb.2004.12.024
volume = 346
issue = 3
pages = 789-800
last = Sakamoto
first = Yasumitsu
coauthors = Nobutada Tanaka, Tomomi Ichimiya, Tadashi Kurihara, Kazuo T. Nakamura
title = Crystal Structure of the Catalytic Fragment of Human Brain 2',3'-Cyclic-nucleotide 3'-Phosphodiesterase
journal = Journal of Molecular Biology
accessdate = 2008-05-14
date = 2005-02-25
url = http://www.sciencedirect.com/science/article/B6WK7-4F3NVYN-2/1/6c6f243346e6740b69de7883a8d727bd
]

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. [Cite journal
issn = 00223042
volume = 69
issue = 4
pages = 1335-42
last = Kasama-Yoshida
first = H
coauthors = Y Tohyama, T Kurihara, M Sakuma, H Kojima, Y Tamai
title = A comparative study of 2',3'-cyclic-nucleotide 3'-phosphodiesterase in vertebrates: cDNA cloning and amino acid sequences for chicken and bullfrog enzymes
journal = Journal of neurochemistry
date = 1997-10
] CNP is thought to play a critical role in the events leading up to myelination. [Cite journal
doi = 10.1006/mcne.1996.0033
volume = 7
issue = 6
pages = 453-466
last = Gravel
first = Michel
coauthors = John Peterson, Voon Wee Yong, Vicky Kottis, Bruce Trapp, Peter E. Braun
title = Overexpression of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase in Transgenic Mice Alters Oligodendrocyte Development and Produces Aberrant Myelination
journal = Molecular and Cellular Neuroscience
accessdate = 2008-05-11
date = 1996-06
url = 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
]

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. [Cite journal
doi = 10.1073/pnas.042678799
volume = 99
issue = 4
pages = 1807-1812
last = Bifulco
first = Maurizio
coauthors = Chiara Laezza, Stefania Stingo, J. Wolff
title = 2',3'-Cyclic nucleotide 3'-phosphodiesterase: A membrane-bound, microtubule-associated protein and membrane anchor for tubulin
journal = Proceedings of the National Academy of Sciences
accessdate = 2008-05-11
date = 2002-02-19
url = http://www.pnas.org/cgi/content/abstract/99/4/1807
]

External Links

* [http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=protein&val=1705945 NCBI Protein]

References


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