TY - JOUR
T1 - Domain analysis of human transmembrane guanylyl cyclase receptors
T2 - implications for regulation.
AU - Potter, Lincoln Ross
PY - 2005
Y1 - 2005
N2 - In the human genome, sequence analysis indicates there are five functional transmembrane guanylyl cyclases, enzymes that synthesize the intracellular second messenger, cGMP. Two, GC-A and GC-B or NPR-A and NPR-B, are widely distributed receptors for atrial natriuretic peptide, brain natriuretic peptide and C-type natriuretic peptide, more commonly known as ANP, BNP and CNP, respectively. One cyclase, GC-C or StaR, is predominantly found in the intestinal epithelium and is the receptor for guanylin and uroguanylin, as well as for the bacterial pathogen, heat-stable enterotoxin (Sta). The remaining two cyclases, GC-E and GC-F or RetGC-1 and RetGC-2, are expressed in the retina and regulate the dark cycle of phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. All five members consist of an extracellular ligand binding domain, single transmembrane spanning domain, and intracellular kinase homology, dimerization and guanylyl cyclase catalytic domains. In the first part of this review, the tissue expression, ligands and "knockout" phenotypes of each receptor are summarized and individual domains are compared. In the second part, regulation by ATP, calcium, protein kinase C and phosphorylation is discussed.
AB - In the human genome, sequence analysis indicates there are five functional transmembrane guanylyl cyclases, enzymes that synthesize the intracellular second messenger, cGMP. Two, GC-A and GC-B or NPR-A and NPR-B, are widely distributed receptors for atrial natriuretic peptide, brain natriuretic peptide and C-type natriuretic peptide, more commonly known as ANP, BNP and CNP, respectively. One cyclase, GC-C or StaR, is predominantly found in the intestinal epithelium and is the receptor for guanylin and uroguanylin, as well as for the bacterial pathogen, heat-stable enterotoxin (Sta). The remaining two cyclases, GC-E and GC-F or RetGC-1 and RetGC-2, are expressed in the retina and regulate the dark cycle of phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. All five members consist of an extracellular ligand binding domain, single transmembrane spanning domain, and intracellular kinase homology, dimerization and guanylyl cyclase catalytic domains. In the first part of this review, the tissue expression, ligands and "knockout" phenotypes of each receptor are summarized and individual domains are compared. In the second part, regulation by ATP, calcium, protein kinase C and phosphorylation is discussed.
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U2 - 10.2741/1613
DO - 10.2741/1613
M3 - Review article
C2 - 15769619
AN - SCOPUS:22844434595
SN - 1093-9946
VL - 10
SP - 1205
EP - 1220
JO - Frontiers in bioscience : a journal and virtual library
JF - Frontiers in bioscience : a journal and virtual library
ER -