Skip to main content
OSTI.GOVU.S. Department of Energy Office of Scientific and Technical Information
U.S. Department of Energy
Office of Scientific and Technical Information
 

Light stimulates phosphorylation of two large membrane proteins in frog photoreceptors

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00336a054· OSTI ID:6297785

By photoactivating rhodopsin, light indirectly initiates a series of biochemical reactions within photoreceptors as part of the visual process. The author reports that one of the light-stimulated reactions in bullfrog photoreceptors is the phosphorylation of two previously unreported proteins (220 and 240 kDa). Their phosphorylation by endogenous kinase(s) is readily observed in freshly isolated, fragmented rods. On subcellular fractionation, the labeled proteins copurify with the membranes of the outer segments, from which they cannot be extracted with low ionic strength. They appear to be integral membrane proteins of the disk or plasma membranes. Their light-induced phosphorylation is also observed in intact receptors when excised frog retinas are incubated under in vivo conditions with TSPO4. Thus, appropriate kinase(s) is (are) present within outer segments and presumably is (are) the one(s) responsible for phosphorylation in fragmented cells. In the presence of adenosine 5'-(gamma-(TVS)thiotriphosphate) (( TVS) ATP-gamma-S), light can also stimulate thiophosphorylation, leading to preferential labeling of the 220-kDa protein. On the basis of four criteria the 220-kDa protein appears to correspond to the membrane protein previously identified at the rims of rod disks.

Research Organization:
Marine Biological Lab., Woods Hole, MA
OSTI ID:
6297785
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 15; ISSN BICHA
Country of Publication:
United States
Language:
English

Similar Records

Identification of frog photoreceptor plasma and disk membrane proteins by radioiodination
Journal Article · Mon Mar 23 23:00:00 EST 1987 · Biochemistry; (United States) · OSTI ID:6470450
Light activation of one rhodopsin molecule causes the phosphorylation of hundreds of others. A reaction observed in electropermeabilized frog rod outer segments exposed to dim illumination
Journal Article · Wed Sep 05 00:00:00 EDT 1990 · Journal of Biological Chemistry; (USA) · OSTI ID:6511411
Study of the orientation of retinal in bovine rhodopsin: the use of a photoactivatable retinal analog
Conference · Fri May 01 00:00:00 EDT 1987 · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) · OSTI ID:6180117

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMPHIBIANS
ANIMALS
AQUATIC ORGANISMS
ATP
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
BODY AREAS
CHEMICAL REACTIONS
DAYS LIVING RADIOISOTOPES
ELECTROMAGNETIC RADIATION
ENZYMES
EVEN-ODD NUCLEI
EYES
FACE
FROGS
HEAD
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
NUCLEI
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
ORGANS
OXYGEN COMPOUNDS
PHOSPHATES
PHOSPHORUS 32
PHOSPHORUS COMPOUNDS
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
PHOTOCHEMICAL REACTIONS
PIGMENTS
PROTEINS
RADIATIONS
RADIOISOTOPES
RECEPTORS
RETINA
RHODOPSIN
SENSE ORGANS
SULFUR 35
SULFUR ISOTOPES
TRACER TECHNIQUES
TRANSFERASES
VERTEBRATES
VISIBLE RADIATION