Abstract
G proteins regulate intracellular signaling by coupling a cycle of guanine nucleotide binding and hydrolysis to transient changes of cellular functions. The mechanisms that control the recycling of transducin, the "pacesetting" G protein that regulates mammalian phototransduction, are unclear. We show that a novel retinal specific RGS-motif protein specifically binds to an intermediate conformation involved in GTP hydrolysis by transducin and accelerates phosphate release and the recycling of transducin. This specific interaction further rationalizes the kinetics of the phototransduction cascade and provides a general hypothesis to explain the mechanism of interaction of RGS proteins with other G proteins.
MeSH Terms
Amino Acid Sequence
Animals
Carrier Proteins/chemistry,isolation & purification,metabolism
Cattle
DNA Primers
Eye Proteins/chemistry,isolation & purification,metabolism
GTP Phosphohydrolases/metabolism
GTP-Binding Proteins/metabolism
Guanosine Triphosphate/metabolism
Male
Mice
Molecular Sequence Data
Organ Specificity
Polymerase Chain Reaction
Protein Binding
Protein Conformation
RGS Proteins
Rats
Recombinant Proteins/biosynthesis,isolation & purification,metabolism
Retina/metabolism
Rod Cell Outer Segment/metabolism
Sequence Homology, Amino Acid
Transducin/isolation & purification,metabolism
Chemicals
Carrier Proteins
DNA Primers
Eye Proteins
RGS Proteins
RGS16 protein
Recombinant Proteins
Guanosine Triphosphate
GTP Phosphohydrolases
GTP-Binding Proteins
Transducin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Chen C K
Division of Biology, California Institute of Technology, Pasadena 91125, USA.
Wieland T
Simon M I
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