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High‐resolution structural studies using cryo–electron microscopy have further revealed unique features such as lateral fenestrations that may allow accommodation of lipid mediators and provide molecular insight into the channel’s gating and trafficking."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn diverse cellular contexts, TRPC3 critically contributes to Ca²⁺ homeostasis and downstream signaling. Elevated TRPC3 expression is observed in several pathological settings—including idiopathic pulmonary arterial hypertension and malignant vascular conditions—where it participates in the aberrant proliferation of smooth muscle and endothelial cells. In cancer cells (such as ovarian and prostate carcinomas) and in immunocytes (including T‐ and B‐lymphocytes), TRPC3‐mediated Ca²⁺ and Na⁺ influx underlies proliferative and differentiation signals. Moreover, in polarized epithelial cells, myometrial tissue, kidney mesangial cells, and even in specialized mitochondrial compartments, TRPC3 plays distinct roles in regulating Ca²⁺ entry, interacting with partners such as Na⁺/Ca²⁺ exchangers and Ca²⁺–activated K⁺ channels to influence contractile, secretory, and inflammatory responses. The expression of TRPC3 is also dynamically modulated by mechanical forces such as shear stress as well as metabolic cues, further underscoring its relevance in both normal physiology and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond mediating ion flux, TRPC3 functions as a dynamic signaling integrator through its interactions with scaffolding and regulatory proteins. Its association with partners such as TRPM4 and RACK1 organizes discrete microdomains that govern the spatial and temporal profiles of Ca²⁺ signals, thereby modulating downstream kinase (e.g. ERK1/2) activation and transcriptional programs affecting cell proliferation, differentiation, and even the onset of cellular senescence. This integrative role places TRPC3 at a pivotal junction of diverse signaling networks whose dysregulation contributes to pathophysiological conditions, including premature senescence and related tumor‐promoting secretomes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Mohamed Trebak, Gary St J Bird, Richard R McKay, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Comparison of human TRPC3 channels in receptor-activated and store-operated modes. 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