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Sci. STKE, 30 January 2001
Vol. 2001, Issue 67, p. tw4
[DOI: 10.1126/stke.2001.67.tw4]


Phospholipase C Ras Targets Phospholipase C

The family of phospholipase C (PLC) isoforms can be divided into three classes β, {gamma}, and {delta}. Song et al. have identified a fourth class of PLC, PLC{varepsilon}, which has sequence similarity to the Caenorhabditis elegans PLC210, including two putative Ras-interacting domains (CDC25-like domain and an RA domain). However, it lacks the conserved pleckstrin homology domain and EF-hand domains of all other classes of PLC. Analysis of recombinant PLC{varepsilon} showed that the protein has phospholipase C activity with a dependence on calcium similar to that of other PLC isoforms. PLC{varepsilon} interacted with the guanosine triphosphatases Ras and Rap1, and this interaction led to the recruitment of PLC{varepsilon} to the plasma membrane or the perinuclear region, respectively, in cells transfected with a green fluorescent protein (GFP)-tagged PLC{varepsilon} and activated forms of Ras or Rap1. Furthermore, the translocation of PLC{varepsilon} to membranes was stimulated in cells treated with epidermal growth factor, and this effect was blocked by expression of dominant negative Ras, supporting the model that Ras recruits the PLC{varepsilon} to the membrane in response to external stimuli.

C. Song, C.-D. Hu, M. Misago, K.-i. Kariya, Y. Yamawaki-Kataoka, M. Shibatohge, D. Wu, T. Satoh, T. Katoaka, Regulation of a novel human phospholipase C, PLC{varepsilon}, through membrane targeting by Ras. J. Biol. Chem. 276, 2752-2757 (2001). [Abstract] [Full Text]

Citation: Ras Targets Phospholipase C. Sci. STKE 2001, tw4 (2001).

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