{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPRKAR1A encodes the type Iα regulatory subunit of cyclic AMP–dependent protein kinase A (PKA), a pivotal mediator of cAMP signaling that controls the activity of the catalytic subunits by forming an inactive holoenzyme complex under basal conditions. On binding of cAMP, a conformational change releases the catalytic subunits to phosphorylate target proteins, thereby ensuring precise spatial and temporal regulation of cellular processes such as hormone responsiveness and cell proliferation. In normal physiology, this mechanism contributes to proper endocrine function and signal compartmentation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations affecting PRKAR1A—whether through inactivating changes that lead to haploinsufficiency or through the expression of aberrant proteins with impaired binding to cAMP or the catalytic subunit—undermine its regulatory function and result in dysregulated PKA activity. Such alterations are central to the pathogenesis of Carney complex and related disorders such as primary pigmented nodular adrenocortical disease (PPNAD), acrodysostosis, and various neoplasms, including thyroid, melanocytic, and pituitary tumors. The loss or alteration of normal PRKAR1A function leads to enhanced cAMP responsiveness, misactivation of downstream signaling cascades (for example, MAPK, mTOR, and TGFβ pathways), and compromised processes such as autophagy, collectively promoting uncontrolled cell proliferation and tumorigenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in regulating PKA catalytic activity, PRKAR1A is emerging as a multifaceted protein that influences cellular compartmentation and a variety of biological processes. Recent studies have demonstrated that PRKAR1A can undergo liquid–liquid phase separation to form biomolecular condensates that spatially organize cAMP and kinase activity, thereby fine‐tuning downstream signaling events. In addition, modulation of PRKAR1A levels has been linked to alterations in cell cycle progression, apoptosis, and cell migration, with implications for fertility, neural function, and the development of diverse human cancers. 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