N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana. Otterhag, L., Sommarin, M., & Pical, C. FEBS Letters, 497(2-3):165–170, 2001. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2801%2902453-X![N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Phosphoinositide-specific phospholipase C's (PI-PLCs) are ubiquitous in eukaryotes, from plants to animals, and catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate into the two second messengers inositol 1,4,5-trisphosphate and diacylglycerol. In animals, four distinct subfamilies of PI-PLCs have been identified, and the three-dimensional structure of one rat isozyme, PLC-δ1, determined. Plants appear to contain only one gene family encoding PI-PLCs. The catalytic properties of plant PI-PLCs are very similar to those of animal enzymes. However, very little is known about the regulation of plant PI-PLCs. All plant PI-PLCs comprise three domains, X, Y and C2, which are also conserved in isoforms from animals and yeast. We here show that one PI-PLC isozyme from Arabidopsis thaliana, AtPLC2, is predominantly localized in the plasma membrane, and that the conserved N-terminal domain may represent an EF-hand domain that is required for catalytic activity but not for lipid binding.
@article{otterhag_n-terminal_2001,
title = {N-terminal {EF}-hand-like domain is required for phosphoinositide-specific phospholipase {C} activity in {Arabidopsis} thaliana},
volume = {497},
copyright = {FEBS Letters 497 (2001) 1873-3468 © 2015 Federation of European Biochemical Societies},
issn = {1873-3468},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1016/S0014-5793%2801%2902453-X},
doi = {10/dv4dn5},
abstract = {Phosphoinositide-specific phospholipase C's (PI-PLCs) are ubiquitous in eukaryotes, from plants to animals, and catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate into the two second messengers inositol 1,4,5-trisphosphate and diacylglycerol. In animals, four distinct subfamilies of PI-PLCs have been identified, and the three-dimensional structure of one rat isozyme, PLC-δ1, determined. Plants appear to contain only one gene family encoding PI-PLCs. The catalytic properties of plant PI-PLCs are very similar to those of animal enzymes. However, very little is known about the regulation of plant PI-PLCs. All plant PI-PLCs comprise three domains, X, Y and C2, which are also conserved in isoforms from animals and yeast. We here show that one PI-PLC isozyme from Arabidopsis thaliana, AtPLC2, is predominantly localized in the plasma membrane, and that the conserved N-terminal domain may represent an EF-hand domain that is required for catalytic activity but not for lipid binding.},
language = {en},
number = {2-3},
urldate = {2021-11-02},
journal = {FEBS Letters},
author = {Otterhag, Lotta and Sommarin, Marianne and Pical, Christophe},
year = {2001},
note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793\%2801\%2902453-X},
keywords = {5)P2, 5-bisphosphate, Arabidopsis thaliana, EF-hand, PH, PI-PLC, Phosphoinositide, Phosphoinositide-specific phospholipase C, Plasma membrane, PtdIns, PtdIns(4, phosphatidylinositol, phosphatidylinositol 4, phosphoinositide-specific phospholipase C, pleckstrin homology},
pages = {165--170},
}
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In animals, four distinct subfamilies of PI-PLCs have been identified, and the three-dimensional structure of one rat isozyme, PLC-δ1, determined. Plants appear to contain only one gene family encoding PI-PLCs. The catalytic properties of plant PI-PLCs are very similar to those of animal enzymes. However, very little is known about the regulation of plant PI-PLCs. All plant PI-PLCs comprise three domains, X, Y and C2, which are also conserved in isoforms from animals and yeast. 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