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Role of phospholipase C in Dictyostelium: formation of inositol 1,4,5‐trisphosphate and normal development in cells lacking phospholipase C activity.
Author(s) -
Drayer A.L.,
Van der Kaay J.,
Mayr G.W.,
Van Haastert P.J.
Publication year - 1994
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1994.tb06423.x
Subject(s) - inositol , library science , biochemistry , biology , bioinformatics , computer science , receptor
The micro‐organism Dictyostelium uses extracellular cAMP to induce chemotaxis and cell differentiation. Signals are transduced via surface receptors, which activate G proteins, to effector enzymes. The deduced protein sequence of Dictyostelium discoideum phosphatidylinositol‐specific phospholipase C (PLC) shows strong homology with the mammalian PLC‐delta isoforms. To study the role of PLC in Dictyostelium, a plc‐ mutant was constructed by disruption of the PLC gene. No basal or stimulated PLC activity could be measured during the whole developmental programme of the plc‐ cells. Loss of PLC activity did not result in a visible alteration of growth or development. Further analysis showed that developmental gene regulation, cAMP‐mediated chemotaxis and activation of guanylyl and adenylyl cyclase were normal. Although the cells lack PLC activity, inositol 1,4,5‐trisphosphate [Ins(1,4,5)P3] was present at only slightly lower concentrations compared with control cells. Mass analysis of inositol phosphates demonstrated the presence of a broad spectrum of inositol phosphates in Dictyostelium, which was unaltered in the plc‐ mutant. Cell labelling experiments with [3H]inositol indicated that [3H]Ins(1,4,5)P3 was formed in a different manner in the mutant than in control cells.