{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T11:54:14Z","timestamp":1791287654215,"version":"4.1.0"},"reference-count":98,"publisher":"The Endocrine Society","issue":"12","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,12,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The type 1\u03b1 regulatory subunit (RI\u03b1) of cAMP-dependent protein kinase (PKA) (coded by the PRKAR1A gene) is the main component of type I PKA, which regulates most of the serine-threonine kinase activity catalyzed by the PKA holoenzyme in response to cAMP. Carney complex (CNC), or the complex of spotty skin pigmentation, myxomas, and endocrine overactivity, is a multiple endocrine (and not only) neoplasia syndrome that is due to PRKAR1A-inactivating mutations. The R1\u03b1 protein and PRKAR1A mRNA have been found to be up-regulated in a series of cell lines and human and rodent neoplasms, suggesting this molecule\u2019s involvement in tumorigenesis and its potential role in cell cycle regulation, growth, and\/or proliferation. Alterations in PKA activity elicit a variety of effects depending on the tissue, developmental stage, degree of differentiation, and cAMP levels. In addition, RI\u03b1 may have functions independent of PKA. The presence of inactivating germline mutations and the loss of its wild-type allele in some CNC lesions indicate that PRKAR1A might function as a tumor suppressor gene in these tissues, but could PRKAR1A be a classic tumor suppressor gene? Probably not, and this review explains why.<\/jats:p>","DOI":"10.1210\/en.2004-0900","type":"journal-article","created":{"date-parts":[[2004,8,27]],"date-time":"2004-08-27T00:23:11Z","timestamp":1093566191000},"page":"5452-5458","source":"Crossref","is-referenced-by-count":176,"title":["Minireview: PRKAR1A: Normal and Abnormal Functions"],"prefix":"10.1210","volume":"145","author":[{"given":"Ioannis","family":"Bossis","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Constantine A.","family":"Stratakis","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"80","reference":[{"key":"2020071613165588400_R1","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0163-7258(91)90075-W","article-title":"Cyclic nucleotide-dependent protein kinases.","volume":"50","author":"Scott","year":"1991","journal-title":"Pharmacol Ther"},{"key":"2020071613165588400_R2","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/1040-8428(94)00166-9","article-title":"cAMP-dependent protein kinase: role in normal and malignant growth.","volume":"21","author":"Cho-Chung","year":"1995","journal-title":"Crit Rev Oncol Hematol"},{"key":"2020071613165588400_R3","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1080\/10408369991239213","article-title":"Cyclic nucleotide-dependent protein kinases: intracellular receptors for cAMP and cGMP action.","volume":"36","author":"Francis","year":"1999","journal-title":"Crit Rev Clin Lab Sci"},{"key":"2020071613165588400_R4","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/S0163-7258(98)00056-4","article-title":"Protein phosphorylation and signal transduction.","volume":"82","author":"Graves","year":"1999","journal-title":"Pharmacol Ther"},{"key":"2020071613165588400_R5","first-page":"D678","article-title":"Specificity in the cAMP\/PKA signaling pathway","volume":"5","author":"Skalhegg","year":"2000","journal-title":"Differential expression, regulation, and subcellular localization of subunits of PKA. 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