Journal article
A site on rod G protein α subunit that mediates effector activation
Science (American Association for the Advancement of Science), Vol.256(5059), pp.1031-1033
1992
DOI: 10.1126/science.1317058
PMID: 1317058
Abstract
The heterotrimeric guanine nucleotide binding proteins (G proteins) are activated by sensory or hormone receptors. In turn, the G proteins activate effector proteins such as adenylyl cyclase, cyclic guanosine 3′,5′-monophosphate phosphodiesterase (cGMP PDE), phospholipase C, and potassium and calcium ion channels by mechanisms that are poorly understood. A site on the α subunit of the G protein transducin (αt) has been identified that interacts with and activates cGMP phosphodiesterase, the effector enzyme in rod photoreceptors. A 22-amino acid peptide, corresponding to residues 293 to 314 from the COOH-terminal region of αt, fully mimicked αt and potently activated PDE. This region is adjacent to the receptor activation domain; thus, the α subunit of this G protein has a site for interaction with both its effector and receptor that maps near the COOH-terminus.
Details
- Title: Subtitle
- A site on rod G protein α subunit that mediates effector activation
- Creators
- Helen M Rarick - University of Illinois at ChicagoNikolai O Artemyev - Univ. Illinois coll. medicine Chicago, dep. physiology biophysics, Chicago IL 60680, United StatesHeidi E Hamm - University of Illinois at Chicago
- Resource Type
- Journal article
- Publication Details
- Science (American Association for the Advancement of Science), Vol.256(5059), pp.1031-1033
- Publisher
- American Association for the Advancement of Science; Washington, DC
- DOI
- 10.1126/science.1317058
- PMID
- 1317058
- ISSN
- 0036-8075
- eISSN
- 1095-9203
- Language
- English
- Date published
- 1992
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Ophthalmology and Visual Sciences
- Record Identifier
- 9984070748802771
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