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They are evolutionarily conserved from sea urchins to humans and regulate diverse physiologies. Most family members are phosphorylated on 4 to 7 conserved serines or threonines at the beginning of their kinase homology domains. This review describes studies that demonstrate that phosphorylation and dephosphorylation are required for activation and inactivation of these enzymes, respectively. Phosphorylation sites in GC-A, GC-B, GC-E, and sea urchin receptors are discussed, as are mutant receptors that mimic the dephosphorylated inactive or phosphorylated active forms of GC-A and GC-B, respectively. A salt bridge model is described that explains why phosphorylation is required for enzyme activation. Potential kinases, phosphatases, and ATP regulation of GC receptors are also discussed. Critically, knock-in mice with glutamate substitutions for receptor phosphorylation sites are described. The inability of opposing signaling pathways to inhibit cGMP synthesis in mice where GC-A or GC-B cannot be dephosphorylated demonstrates the necessity of receptor dephosphorylation in vivo. Cardiac hypertrophy, oocyte meiosis, long-bone growth\/achondroplasia, and bone density are regulated by GC phosphorylation, but additional processes are likely to be identified in the future.<\/jats:p>","DOI":"10.1210\/endrev\/bnae015","type":"journal-article","created":{"date-parts":[[2024,5,7]],"date-time":"2024-05-07T14:12:07Z","timestamp":1715091127000},"page":"755-771","source":"Crossref","is-referenced-by-count":9,"title":["Phosphorylation-Dependent Regulation of Guanylyl Cyclase (GC)-A and Other Membrane GC Receptors"],"prefix":"10.1210","volume":"45","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6461-4288","authenticated-orcid":false,"given":"Lincoln R","family":"Potter","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Medical School , Minneapolis, MN 55455 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"80","published-online":{"date-parts":[[2024,5,7]]},"reference":[{"issue":"23","key":"2024091719341144900_bnae015-B1","doi-asserted-by":"crossref","first-page":"6363","DOI":"10.1016\/S0021-9258(18)63473-8","article-title":"Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3',5'-monophosphate from guanosine trihosphate","volume":"244","author":"Hardman","year":"1969","journal-title":"J Biol Chem"},{"issue":"23","key":"2024091719341144900_bnae015-B2","doi-asserted-by":"crossref","first-page":"6371","DOI":"10.1016\/S0021-9258(18)63474-X","article-title":"Determination of guanosine 3',5'-monophosphate in tissues and of guanyl cyclase in rat intestine","volume":"244","author":"Ishikawa","year":"1969","journal-title":"J Biol Chem"},{"issue":"3","key":"2024091719341144900_bnae015-B3","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1016\/0005-2744(69)90362-3","article-title":"Detection of guanyl cyclase in mammalian tissues","volume":"191","author":"White","year":"1969","journal-title":"Biochim Biophys Acta"},{"issue":"24","key":"2024091719341144900_bnae015-B4","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1016\/0024-3205(69)90189-1","article-title":"Guanyl cyclase. 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