Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins.
Effects of aluminum, magnesium, and fluoride (AMF) on members of both the trimeric G protein and smaller (20-25 kDa) monomeric GTP-binding protein families were examined. The dissociation of GDP from G proteins was blocked by AMF but was unchanged with the addition of AMF to any of six of the monomeric GTP-binding proteins. Biochemical activities and properties of one of the smaller GTP-binding proteins, ADP-ribosylation factor, were also found to be unaffected by AMF. It is concluded that the ability of AMF to activate the trimeric G proteins is not shared by the smaller GTP-binding proteins and thus should prove to be a useful discriminator between cellular activities regulated by these two families of regulatory proteins.
Kahn
R A
RA
Laboratory of Biological Chemistry, National Cancer Institute, Bethesda, Maryland 20892.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000535:Aluminum / Q000737:chemistry*; D000818:Animals; D001921:Brain / Q000378:metabolism; D002384:Catalysis; D002417:Cattle; D005459:Fluorides / Q000737:chemistry*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D008274:Magnesium / Q000737:chemistry*; D008970:Molecular Weight
D000246:Adenosine Diphosphate Ribose; D000535:Aluminum; D019204:GTP-Binding Proteins; D008274:Magnesium; D005459:Fluorides