Structure and biological function of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-08

AUTHORS

Junko Morita, Kuniyuki Kano, Kazuki Kato, Hiroyuki Takita, Hideki Sakagami, Yasuo Yamamoto, Emiko Mihara, Hirofumi Ueda, Takanao Sato, Hidetoshi Tokuyama, Hiroyuki Arai, Hiroaki Asou, Junichi Takagi, Ryuichiro Ishitani, Hiroshi Nishimasu, Osamu Nureki, Junken Aoki

ABSTRACT

Choline is an essential nutrient for all living cells and is produced extracellularly by sequential degradation of phosphatidylcholine (PC). However, little is known about how choline is produced extracellularly. Here, we report that ENPP6, a choline-specific phosphodiesterase, hydrolyzes glycerophosphocholine (GPC), a degradation product of PC, as a physiological substrate and participates in choline metabolism. ENPP6 is highly expressed in liver sinusoidal endothelial cells and developing oligodendrocytes, which actively incorporate choline and synthesize PC. ENPP6-deficient mice exhibited fatty liver and hypomyelination, well known choline-deficient phenotypes. The choline moiety of GPC was incorporated into PC in an ENPP6-dependent manner both in vivo and in vitro. The crystal structure of ENPP6 in complex with phosphocholine revealed that the choline moiety of the phosphocholine is recognized by a choline-binding pocket formed by conserved aromatic and acidic residues. The present study provides the molecular basis for ENPP6-mediated choline metabolism at atomic, cellular and tissue levels. More... »

PAGES

20995

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep20995

DOI

http://dx.doi.org/10.1038/srep20995

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052584605

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26888014


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