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Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C

Nature volume 332, pages 457–459 (1988)Cite this article

Abstract

Membrane anchoring of proteins by a covalently attached glycosyl-phosphatidylinositol moiety has been reported in many different eukaryotic cells including parasite protozoa1–5. The diversity of proteins in which this phospholipid attachment is found suggests that it is functionally important and perhaps also functionally pleiotropic. Studies on the Thy-1 antigen of murine lymphocytes6 indicate that it can facilitate the lateral mobility of membrane proteins. It can also permit the rapid and specific release of the anchored proteins from the membrane following cleavage by a phosphatidyl inositol-specific phospholipase C (PI-PLC)7,8. Here we show that this type of anchoring may be involved in the regulation of an enzymatic activity. PI-PLC releases a Plasmodium falciparum membrane protein of relative molecular mass (Mr) 76K (p76) from intact merozoites or isolated schizont membranes and induces a proteolytic activity associated with its soluble form. Endogenous activation of the proteolytic activity of p76 appears to occur at the end of the schizogony and could initiate a cascade of biochemical events associated with merozoite maturation.

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Authors and Affiliations

  1. Unite de Parasitologie experimentale * and Unite de Biologic des membranes†, Institut Pasteur, 75724, Paris, Cedex 15, France

    Catherine Braun-Breton & Luiz Pereira da Silva

  2. Department of Pharmacology, Case Western Reserve University, Cleveland, Ohio, 44106, USA

    Terrone L. Rosenberry

Authors
  1. Catherine Braun-Breton
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  2. Terrone L. Rosenberry
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  3. Luiz Pereira da Silva
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Braun-Breton, C., Rosenberry, T. & da Silva, L. Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C. Nature 332, 457–459 (1988). https://doi.org/10.1038/332457a0

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