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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Multiple roles of phosphoinositide-specific phospholipase C isozymes

  • Suh, Pann-Ghill (Division of Molecular and Life Sciences, Pohang University of Science and Technology) ;
  • Park, Jae-Il (Division of Molecular and Life Sciences, Pohang University of Science and Technology) ;
  • Manzoli, Lucia (Cellular Signaling Laboratory, Department of Anatomical Sciences, University of Bologna) ;
  • Cocco, Lucio (Cellular Signaling Laboratory, Department of Anatomical Sciences, University of Bologna) ;
  • Peak, Joanna C. (Cancer Research UK Centre for Cell and Molecular Biology, Chester Beatty Laboratories, The Institute of Cancer Research) ;
  • Katan, Matilda (Cancer Research UK Centre for Cell and Molecular Biology, Chester Beatty Laboratories, The Institute of Cancer Research) ;
  • Fukami, Kiyoko (Laboratory of Genome and Biosignal, Tokyo University of Pharmacy and Life Science) ;
  • Kataoka, Tohru (Division of Molecular Biology, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine) ;
  • Yun, Sang-Uk (Division of Molecular and Life Sciences, Pohang University of Science and Technology) ;
  • Ryu, Sung-Ho (Division of Molecular and Life Sciences, Pohang University of Science and Technology)
  • Accepted : 2008.06.03
  • Published : 2008.06.30
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Abstract

Phosphoinositide-specific phospholipase C is an effector molecule in the signal transduction process. It generates two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. Currently, thirteen mammal PLC isozymes have been identified, and they are divided into six groups: PLC-$\beta$, -$\gamma$, -$\delta$, -$\varepsilon$, -$\zeta$ and -$\eta$. Sequence analysis studies demonstrated that each isozyme has more than one alternative splicing variant. PLC isozymes contain the X and Y domains that are responsible for catalytic activity. Several other domains including the PH domain, the C2 domain and EF hand motifs are involved in various biological functions of PLC isozymes as signaling proteins. The distribution of PLC isozymes is tissue and organ specific. Recent studies on isolated cells and knockout mice depleted of PLC isozymes have revealed their distinct phenotypes. Given the specificity in distribution and cellular localization, it is clear that each PLC isozyme bears a unique function in the modulation of physiological responses. In this review, we discuss the structural organization, enzymatic properties and molecular diversity of PLC splicing variants and study functional and physiological roles of each isozyme.

Keywords

References

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