CUB domain-containing protein 1 (CDCP1) (CDCP1)

CUB domain-containing protein 1 (CDCP1), also known as CD318 or TRASK, is a type I transmembrane glycoprotein that serves as a critical regulator of cell adhesion and signaling [1, 3]. It contains three extracellular CUB domains (the ectodomain) and an intracellular domain with multiple tyrosine phosphorylation sites [2, 6]. In cancer, CDCP1 is frequently overexpressed and undergoes proteolytic cleavage by serine proteases, which triggers its phosphorylation by Src family kinases [2, 9]. This activation promotes oncogenic signaling through the PI3K/AKT and MAPK pathways, facilitating tumor cell migration, invasion, and resistance to anoikis [6, 9]. Due to its high expression in aggressive malignancies like triple-negative breast cancer, lung adenocarcinoma, and metastatic prostate cancer, the CDCP1 ectodomain has become a prominent target for therapeutic interventions, including antibody-drug conjugates (ADCs), radioligand therapies, and bispecific antibodies [7, 11, 14].

Other names

CD318SIMA135TRASKgp140Membrane glycoprotein gp140Subtractive immunization M plus HEp3-associated 135 kDa proteinTransmembrane and associated with src kinases

Antibody-drug conjugate (ADC) mediated cytotoxicity, radioligand therapy (RLT), inhibition of Src-mediated phosphorylation, induction of target internalization and degradation, and blocking of protein-protein interactions.