'Cap' structures in maize poly(A)-containing RNA.

Receptor regulation of phosphoinositidase C.

Numerous hormones, neurotransmitters and growth factors regulate intracellular events by acting at cell surface receptors which are coupled to the generation of inositol phospholipid-derived intracellular messengers. Receptors trigger the hydrolysis of inositol phospholipids by activating phosphoinositidase C (PIC) enzymes. At least four families of genes encode structurally distinct PIC enzymes and it is likely that distinct PIC isoenzymes participate in different pathways of signal transduction. Two different modes of receptor regulation have been identified and these involve distinct PIC isoenzymes. In the first of these, PIC-gamma is a substrate for growth factor receptor protein-tyrosine kinases. The second of these pathways involves PIC-beta plus other isoenzymes whose activities are regulated by G proteins in response to agonist binding to G protein-linked receptors. At least two types of G proteins regulate PIC activity and each may control the activity of different PIC isoenzymes.