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Papers In Press, published online ahead of print June 17, 2002
HHMI/Biochemistry, MS-140, Rice University, Houston, TX 77005-1892
Corresponding Author: richard{at}bioc.rice.edu
In Dictyostelium discoideum, cell density is monitored by levels of a secreted protein, conditioned-medium factor (CMF). CMFR1 is a putative CMF receptor necessary for CMF-induced G protein-independent accumulation of the SP70 prespore protein, but not for CMF-induced G protein-dependent IP3 production. Using recombinant fragments of CMF, we find that stimulation of the IP3 pathway requires amino acids 170 – 180 whereas SP70 accumulation does not, corroborating a two-receptor model. Cells lacking CMFR1 do not aggregate, due to the lack of expression of several important early developmentally regulated genes, including gp80. Although many aspects of early developmental cAMP-stimulated signal transduction are mediated by CMF, CMFR1 is not essential for cAMP-stimulated cAMP and cGMP production or Ca++ uptake, suggesting the involvement of a second CMF receptor. Exogenous application of antibodies against either the region between a first and second or a second and third possible transmembrane domain of CMFR1 induces SP70 accumulation. Antibody- and CMF-induced gene expression can be inhibited by recombinant CMFR1 corresponding to the region between the first and third potential transmembrane domains, indicating that this region is extracellular and likely contains the CMF binding site. These observations support a model where a one- or two-transmembrane CMFR1 regulates gene expression and a G protein-coupled CMF receptor mediates cAR1 signal transduction.
J. Biol. Chem, 10.1074/jbc.M204539200
Submitted on May 8, 2002
Revised on June 13, 2002
Accepted on June 17, 2002
A single cell-density sensing factor stimulates distinct signal transduction pathways through two different receptors
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