{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNck1 is a versatile adaptor protein that couples tyrosine‐phosphorylation events at a variety of receptor complexes to the dynamic regulation of the actin cytoskeleton. In multiple contexts—including immune receptor signaling, podocyte slit diaphragm formation, and pathogen‐induced actin rearrangements—Nck1 binds phosphorylated motifs (or exposes binding motifs when these are unphosphorylated) on proteins such as WAVE1, N‑WASP, nephrin, and CD3ε. These interactions mediate the nucleation of actin filaments, promote the assembly of multiprotein complexes (for example, those involving SLP‑76 and VAV1 in T cells), and coordinate the formation of specialized membrane structures such as invadopodia, pedestals, and actin tails. In addition, Nck1 participates in linking receptor clustering (e.g. at sites of Nephrin or Tir engagement) to localized actin polymerization, thereby regulating cell polarity, adhesion, and migration."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in orchestrating actin dynamics, Nck1 also influences intracellular signaling pathways that control protein translation, cellular stress responses, and growth. In these settings the adaptor participates in the formation of complexes that regulate eIF2α dephosphorylation and overall translational efficiency, and it modulates kinase cascades downstream of growth factor receptors. For example, Nck1 is found in complexes with c‐Cbl, eIF2 subunits, and phosphatase regulatory proteins to maintain low levels of eIF2α phosphorylation under endoplasmic reticulum stress. Moreover, by associating with Dock proteins and participating in feedback mechanisms in insulin receptor signaling and FGF‑2–mediated pathways, Nck1 helps fine‑tune intracellular responses that impact cell cycle progression and survival."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurthermore, Nck1 plays pivotal roles in pathological processes including aberrant cell migration, angiogenesis, inflammation, and tumor progression. By integrating signals from growth factors such as VEGF and PDGF, from oncogenic kinases like Bcr‑Abl and STAT3, and from pathogen–host interactions (as seen in enteropathogenic Escherichia coli and picornavirus infections), Nck1 contributes to the regulation of endothelial activation, directional migration, and matrix degradation required for invasion and metastasis. In addition, emerging evidence from studies on long noncoding RNAs that modulate Nck1 expression underscores its importance in cancer progression. Collectively, these diverse functions highlight Nck1 as a central node coordinating receptor‐mediated signaling with cytoskeletal reorganization and stress adaptation in both normal physiology and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "37", "end_ref": "50"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sharon Eden, Rajat Rohatgi, Alexandre V Podtelejnikov, et al. 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