Guanylate cyclase receptor family.
The plasma membrane forms of guanylate cyclase contain a highly conserved catalytic domain, which is also conserved in the soluble form of the enzyme and in mammalian adenylate cyclase. A protein kinase-like domain lies to the amino-terminal side of the catalytic domain and appears to be required for signaling via cGMP; it might also signal, itself, through phosphotransferase activity. This domain is present in the growth factor receptors, but appears not to be a component of other guanylate cyclases or adenylate cyclases. A single transmembrane domain then separates the cyclase catalytic and protein kinase-like domains from the putative ligand-binding domain. At least two plasma membrane forms of gunaylate cyclase (i.e., GC-A and GC-B) have now been identified, and their ligand specificities appear to be distinctly different. The tissue/cellular distribution of this family of receptors is now of potential importance, since specific agonists might differentially regulate physiological processes via the secondary messenger, cGMP, dependent on cellular distribution of the receptors.
Garbers
D L
DL
Department of Pharmacology, Howard Hughes Medical Institute, Vanderbilt University Medical Center, Nashville, Tennessee 37232.
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D004789:Enzyme Activation; D005786:Gene Expression Regulation; D006162:Guanylate Cyclase / Q000235:genetics / Q000502:physiology; D008297:Male; D008969:Molecular Sequence Data; D012617:Sea Urchins; D013094:Spermatozoa / Q000201:enzymology
D006162:Guanylate Cyclase