{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMAPKAP1 (also known as Sin1 or SAPK‐interacting protein 1) is a core, evolutionarily conserved scaffold that orchestrates the assembly and activity of mTOR complex 2 (mTORC2). It is required for the full phosphorylation of key downstream kinases such as Akt at Ser473 and SGK1, thereby regulating essential processes including cell survival, metabolism, cytoskeletal organization, and stress‐responsive signaling. Structural and biochemical studies have revealed that MAPKAP1 contains functional domains (e.g. a pleckstrin homology domain and a Ras-binding domain) that enable its interaction with a variety of protein kinases and regulatory factors. These interactions permit MAPKAP1 not only to support the structural integrity of mTORC2 (through binding with partners such as rictor and mTOR) but also to confer substrate specificity. In addition, MAPKAP1 directly interacts with other signaling effectors—for example, it associates with SGK1 to regulate ion transport, with MEKK2 to modulate MAP kinase cascades, and with PCBP2 in antiapoptotic responses—demonstrating its multifaceted roles as a signaling adaptor."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its central role in mTORC2 assembly, MAPKAP1 is subject to multiple layers of regulation that fine-tune its downstream signaling. Its own activity can be modulated by phosphorylation events—such as Akt-mediated phosphorylation of MAPKAP1—which in turn stimulate a positive feedback loop that further enhances mTORC2 activity. In parallel, translational control mechanisms (for example, suppression by Pdcd4) and post-translational stabilization via LPA/JNK signaling influence MAPKAP1 protein levels and subcellular localization (including at the plasma membrane, mitochondria, and specific endosomes). In addition, MAPKAP1 contributes to immune receptor signaling, as it is required for full IFNγ-mediated Akt activation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of MAPKAP1 has been implicated in a wide spectrum of pathological conditions. Genetic and epigenetic alterations—including enhancer variants and microRNA-mediated targeting (for example, by miR-611)—modulate its expression in various cancers such as non–small cell lung cancer, breast cancer, prostate cancer, hepatocellular carcinoma, and glioma. In certain settings, aberrant MAPKAP1 activity contributes to enhanced epithelial-to-mesenchymal transition, invasion, and metastasis as well as to altered immune and thrombotic responses (for example, in platelet activation during myocardial infarction and in fibrotic processes). These findings have not only provided mechanistic insights into numerous stress, survival, and differentiation pathways but have also suggested that therapeutic targeting of MAPKAP1 and its regulated mTORC2 signaling axis may have clinical utility."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wayne Schroder, Nicole Cloonan, Gillian Bushell, et al. 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