{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSKP1 is a pivotal adaptor protein that links substrate‐recognition F‑box proteins to the cullin scaffold within SCF (Skp1–Cullin–F‑box) ubiquitin ligases. Structural and biochemical studies have revealed that SKP1 not only stabilizes the SCF assembly but also directly influences substrate recognition and the processivity of polyubiquitination. Crystallographic and solution studies demonstrate how SKP1 facilitates the proper folding of F‑box proteins and helps orient substrates for efficient covalent modification by ubiquitin‐conjugating enzymes. Furthermore, tissue‐specific studies indicate that SKP1-containing SCF complexes can be tailored to distinct cellular environments, such as in the specialized context of the organ of Corti."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThrough its role in the SCF ubiquitin ligase, SKP1 modulates the timely turnover of cell cycle regulators and other critical proteins, thereby sustaining proper cell proliferation and maintaining genomic stability. SKP1‐dependent SCF complexes regulate the degradation of key enzymes involved in glycolysis and chromatin modification and ensure orderly progression through checkpoints by targeting inhibitors and activators alike. Furthermore, malfunction or misregulation of SKP1-containing complexes has been linked to oncogenic transformation, as seen in models of T‑cell lymphoma and dysregulated cyclin degradation, underscoring its importance in cell cycle control and tumor suppression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical function in cell cycle control, SKP1 is also implicated in diverse specialized processes that span host–pathogen interactions, modulation of epithelial–mesenchymal transition, neuronal survival, and even autophagic versus secretory pathways. Pathogenic organisms such as Salmonella and poxviruses subvert the host SCF machinery by directly targeting SKP1, thereby altering inflammatory and immune responses. In addition, SKP1-containing complexes mediate processes that affect cell migration, invasion, and neuronal protein quality control, and have been linked to deregulated ubiquitin–proteasome activity in neurodegenerative diseases and parasitic cell division. These studies collectively highlight the broad impact of SKP1 on ubiquitin-mediated proteolysis and its versatile role in maintaining cellular homeostasis under both physiological and pathological conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Geng Wu, Guozhou Xu, Brenda A Schulman, et al. 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