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A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate

Author

Listed:
  • Lucia E. Rameh

    (Harvard Medical School, Beth Israel Deaconess Medical Center)

  • Kimberley F. Tolias

    (Harvard Medical School, Beth Israel Deaconess Medical Center)

  • Brian C. Duckworth

    (Harvard Medical School, Beth Israel Deaconess Medical Center)

  • Lewis C. Cantley

    (Harvard Medical School, Beth Israel Deaconess Medical Center)

Abstract

Phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2), a key molecule in the phosphoinositide signalling pathway, was thought to be synthesized exclusively by phosphorylation of PtdIns-4-P at the D-5 position of the inositol ring. The enzymes that produce PtdIns-4,5-P2 in vitro fall into two related subfamilies (type I and type II PtdInsP-5-OH kinases, or PIP(5)Ks) based on their enzymatic properties and sequence similarities1. Here we have reinvestigated the substrate specificities of these enzymes. As expected, the type I enzyme phosphorylates PtdIns-4-P at the D-5 position of the inositol ring. Surprisingly, the type II enzyme, which is abundant in some tissues, phosphorylates PtdIns-5-P at the D-4 position, and thus should be considered as a 4-OH kinase, or PIP(4)K. The earlier error in characterizing the activity of the type II enzyme is due to the presence of contaminating PtdIns-5-P in commercial preparations of PtdIns-4-P. Although PtdIns-5-P was previously thought not to exist in vivo, we find evidence for the presence of this lipid in mammalian fibroblasts, establishing a new pathway for PtdIns-4,5-P2 synthesis.

Suggested Citation

  • Lucia E. Rameh & Kimberley F. Tolias & Brian C. Duckworth & Lewis C. Cantley, 1997. "A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate," Nature, Nature, vol. 390(6656), pages 192-196, November.
    • Handle: RePEc:nat:nature:v:390:y:1997:i:6656:d:10.1038_36621
    DOI: 10.1038/36621
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    Cited by:

    1. Alessandro Poli & Fabrizio A. Pennacchio & Andrea Ghisleni & Mariagrazia Gennaro & Margaux Lecacheur & Paulina Nastały & Michele Crestani & Francesca M. Pramotton & Fabio Iannelli & Galina Beznusenko , 2023. "PIP4K2B is mechanoresponsive and controls heterochromatin-driven nuclear softening through UHRF1," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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