Cell density sensing mediated by a G protein-coupled receptor activating phospholipase C.

The Journal of Biological Chemistry
Derrick BrazillR H Gomer

Abstract

When the unicellular eukaryote Dictyostelium discoideum starves, it senses the local density of other starving cells by simultaneously secreting and sensing a glycoprotein called conditioned medium factor (CMF). When the density of starving cells is high, the corresponding high density of CMF permits signal transduction through cAR1, the chemoattractant cAMP receptor. cAR1 activates a heterotrimeric G protein whose alpha-subunit is Galpha2. CMF regulates cAMP signal transduction in part by regulating the lifetime of the cAMP-stimulated Galpha2-GTP configuration. We find here that guanosine 5'-3-O-(thio)triphosphate (GTPgammaS) inhibits the binding of CMF to membranes, suggesting that the putative CMF receptor is coupled to a G protein. Cells lacking Galpha1 (Galpha1 null) do not exhibit GTPgammaS inhibition of CMF binding and do not exhibit CMF regulation of cAMP signal transduction, suggesting that the putative CMF receptor interacts with Galpha1. Work by others has suggested that Galpha1 inhibits phospholipase C (PLC), yet when cells lacking either Galpha1 or PLC were starved at high cell densities (and thus in the presence of CMF), they developed normally and had normal cAMP signal transduction. We find that CMF activates PL...Continue Reading

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Citations

Feb 19, 2002·Molecular and Biochemical Parasitology·Norma MarchesiniEstela E Machado-Domenech
Apr 28, 2011·Development, Growth & Differentiation·Richard H GomerDerrick Brazill
Jul 27, 2007·Critical Reviews in Microbiology·Irina V Shemarova
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Jun 29, 2021·Biophysics and Physicobiology·Udoy S BasakTamiki Komatsuzaki

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