Functional exchange of components between light-activated photoreceptor phosphodiesterase and hormone-activated adenylate cyclase systems

Journal Article · Tue Jun 01 00:00:00 EDT 1982 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.79.11.3408· OSTI ID:6306831

Bitensky, M W; Wheeler, M A; Rasenick, M M; Yamazaki, A; Stein, P J; Halliday, K R; Wheeler, G L

Previous studies have noted profound similarities between the regulation of light-activated (3',5'-cyclic-nucleotide 5'-nucleotidohydrolase, EC 3.1.4.17) in retinal rods and hormone-activated adenylate cyclase (ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1) in a variety of tissues. We report ere the functional exchange of components isolated from the photoreceptor system, which displayed predicted functional characteristics when incubated with recipient adenylate cyclase systems from rat cerebral cortical and hypothalamic synaptic membranes and frog erythrocyte ghosts. We demonstrate functional exchange of photoreceptor components at each of three loci: the hormone receptor, the GTP-binding protein (GBP), and the catalytic moiety of adenylate cyclase. Illuminated (but not unilluminated) rhodopsin was found to mimic the hormone-receptor complex, causing GTP-dependent activation of adenylate cyclase. The photoreceptor GBP complexed with guanosine 5'-(..beta..,..gamma..)imidotriphosphate (p(NH)ppG) produced a marked activation of recipient adenylate cyclase systems. Much smaller activation was observed when GBP was not complexed with p(NH)ppG. A heat-stable photoreceptor phosphodiesterase inhibitor reduced both basal and Mn/sup 2 +/-activated adenylate cyclase activites and this inhibition was reversed by photoreceptor GBPp(NH)ppG. These data demonstrate a remarkable functional compatibility between subunits of both systems and furthermore imply that specialized peptide domains responsible for protein-protein interactions are highly conserved.

• Research Organization: Yale Univ. School of Medicine, New Haven, CT
• OSTI ID: 6306831
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 79
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PHOSPHODIESTERASES
CHEMICAL ACTIVATION
RECEPTORS
ADRENALINE
ATP
CELL MEMBRANES
CEREBRAL CORTEX
ENZYME INHIBITORS
ENZYMES
ERYTHROCYTES
EXPERIMENTAL DATA
FROGS
GUANYLIC ACID
LYASES
MANGANESE
NORADRENALINE
PHOTOCHEMICAL REACTIONS
PIGMENTS
RATS
SEROTONIN
VISION
ADRENAL HORMONES
AMINES
AMPHIBIANS
ANIMALS
AQUATIC ORGANISMS
AUTONOMIC NERVOUS SYSTEM AGENTS
AZOLES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY
BODY FLUIDS
BRAIN
CARDIOTONICS
CARDIOVASCULAR AGENTS
CELL CONSTITUENTS
CENTRAL NERVOUS SYSTEM
CEREBRUM
CHEMICAL REACTIONS
DATA
DRUGS
ELEMENTS
ESTERASES
HETEROCYCLIC COMPOUNDS
HORMONES
HYDROLASES
HYDROXY COMPOUNDS
INDOLES
INFORMATION
MAMMALS
MATERIALS
MEMBRANES
METALS
NERVOUS SYSTEM
NEUROREGULATORS
NUCLEOTIDES
NUMERICAL DATA
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANS
PYRROLES
RADIOPROTECTIVE SUBSTANCES
RODENTS
STEROID HORMONES
SYMPATHOMIMETICS
TRANSITION ELEMENTS
TRYPTAMINES
VERTEBRATES
550200* - Biochemistry