G protein and diacylglycerol regulate metamorphosis of planktonic molluscan larvae.

The regulatory guanine nucleotide binding protein (G protein) activators cholera toxin and the GTP analog 5-guanylyl imidophosphate, the second messenger diacylglycerol, and certain diamino acids all facilitate (amplify) the settlement and metamorphic responses of planktonic larvae of Haliotis rufescens (marine mollusc) to morphogenetic chemical stimuli. In contrast, the G protein-inhibiting analog guanosine 5'-O-[beta-thio]diphosphate inhibits facilitation by L-alpha,beta-diaminopropionic acid but does not block facilitation by diacylglycerol. Diacylglycerol, cholera toxin, and the guanine nucleotide analogs alone neither induce the settlement and metamorphosis of the larvae nor do they inhibit induction of metamorphosis by gamma-aminobutyric acid. These results thus establish the existence of separate regulatory and inductive pathways controlling larval metamorphosis in response to two classes of exogenous chemical signals from the environment. The regulatory pathway, operating independently through a G protein-diacylglycerol cascade apparently controlled by facilitating diamino acids in the water column, can amplify the larval responsiveness to inducers of metamorphosis. This mechanism may have adaptive significance in the recognition and selection of favorable habitats for metamorphosis of the larvae. Similar regulatory pathways, based on exogenous control of a G protein-diacylglycerol cascade, may govern responsiveness to stimuli in other sensory and developmental systems.