{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n CDCP1 is a transmembrane glycoprotein that is frequently overexpressed and aberrantly activated in a wide range of human cancers—including lung, breast, pancreatic, colorectal, gastric, renal, and ovarian carcinomas, as well as in certain leukemias—and its activity is closely linked to tumor progression and metastasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": " CDCP1 functions predominantly as a signaling molecule whose tyrosine phosphorylation—often mediated by Src family kinases—triggers recruitment of effectors such as protein kinase Cδ and results in the activation of downstream pathways that promote cell survival, migration, invasion, and resistance to anoikis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "9"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In several tumor types, proteolytic processing of full‐length (135‐kDa) CDCP1 into a membrane-retained 70‐kDa fragment is a critical step that enhances its pro-metastatic actions. This cleavage event permits CDCP1 to interact with integrins and to activate focal adhesion kinase (FAK) and PI3K/Akt signaling cascades, thereby facilitating tumor cell intravasation, extravasation, and colonization of distant organs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "13"}]}, {"type": "t", "text": " In triple-negative breast cancer, for example, CDCP1 is shown to deplete lipid droplets and promote fatty acid oxidation to meet energetic demands during migration and metastasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Moreover, high CDCP1 expression has been correlated with poor prognosis, increased recurrence, and resistance to conventional therapies. It can modulate signaling cross-talk with other receptor tyrosine kinases—such as EGFR, HER2, and AXL—to confer resistance to targeted agents like tyrosine kinase inhibitors and trastuzumab."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "17"}]}, {"type": "t", "text": " CDCP1 is also expressed by cancer stem cell populations—for instance, in colorectal cancers—where it contributes to organ-specific metastatic behavior by enhancing adhesion to vascular endothelium"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": "and is found on immature hematopoietic as well as other progenitor cell subsets."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Preclinical studies demonstrate that targeting CDCP1 with function-blocking antibodies or inhibitory peptides disrupts its signaling and markedly reduces tumor cell migration, invasion, and metastasis while also inducing apoptosis or sensitizing cells to chemotherapy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "23"}]}, {"type": "t", "text": " In addition, CDCP1 expression is regulated by oncogenic signals such as activated Ras and hypoxia-inducible factors (notably HIF-2α), further linking CDCP1 to aggressive tumor phenotypes and drug resistance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "26"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Collectively, these findings support a central role for CDCP1 as a modulator of pro-survival and pro-metastatic signaling—acting through both its full-length and cleaved forms—to promote tumor cell dissemination, resistance to anoikis, and therapeutic evasion. 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