CTP:phosphocholine cytidylyltransferase: Function, regulation, and structure of an amphitropic enzyme required for membrane biogenesis

Rosemary B. Cornell, Neale D. Ridgway

Producción científica: Contribución a una revistaArtículo de revisiónrevisión exhaustiva

114 Citas (Scopus)

Resumen

Abstract CTP:phosphocholine cytidylyltransferase (CCT) catalyzes a rate-limiting and regulated step in the CDP-choline pathway for the synthesis of phosphatidylcholine (PC) and PC-derived lipids. Control of CCT activity is multi-layered, and includes direct regulation by reversible membrane binding involving a built-in lipid compositional sensor. Thus CCT contributes to phospholipid compositional homeostasis. CCT also modifies the curvature of its target membrane. Knowledge of CCT structure and regulation of its catalytic function are relatively advanced compared to many lipid metabolic enzymes, and are reviewed in detail. Recently the genetic origins of two human developmental and lipogenesis disorders have been traced to mutations in the gene for CCTα.

Idioma originalEnglish
Número de artículo883
Páginas (desde-hasta)147-171
Número de páginas25
PublicaciónProgress in Lipid Research
Volumen59
DOI
EstadoPublished - jul. 27 2015

Nota bibliográfica

Funding Information:
We wish to dedicate this article to Dr. Dennis Vance, our mentor, who introduced us to this fascinating enzyme. His ground-breaking research on the regulation of CCT and its role in PC metabolism set the stage for the questions that we and many others have pursued in our own laboratories. We thank Dr. Svetla Taneva for suggestions on this review. Work in the authors laboratories reviewed here was supported by the Canadian Institutes for Health Research and Natural Sciences and Engineering Research Council (Canada).

Publisher Copyright:
© 2015 Published by Elsevier Ltd.

ASJC Scopus Subject Areas

  • Biochemistry
  • Cell Biology

PubMed: MeSH publication types

  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Review

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