ArticleThe Journal of biological chemistry2010
Proteolysis-induced N-terminal ectodomain shedding of the integral membrane glycoprotein CUB domain-containing protein 1 (CDCP1) is accompanied by tyrosine phosphorylation of its C-terminal domain and recruitment of Src and PKCdelta.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 67 citations in OpenAlex.
- CDCP1-targeted antibody-drug conjugates and immunocytokines for cancer therapy.Cancer chemotherapy and pharmacology · 2026Article
- CDCP1/mitochondrial Src axis increases electron transport chain function to promote metastasis in triple-negative breast cancer.British journal of cancer · 2025Article
- CDCP1 promotes the malignant phenotypes of nasopharyngeal carcinoma via the Wnt/β-catenin signaling pathway.BMC biotechnology · 2025Article
- CUB domain-containing protein 1 signaling dysregulates gemcitabine metabolism contributing to therapeutic resistance in T24 cells.PloS one · 2025Article
- The roles of proteases in prostate cancer.IUBMB life · 2023Review
- Theranostic Targeting of CUB Domain-Containing Protein 1 (CDCP1) in Multiple Subtypes of Bladder Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023Article
- CDCP1 expression is frequently increased in aggressive urothelial carcinoma and promotes urothelial tumor progression.Scientific reports · 2023Article
- CUB Domain-Containing Protein 1 (CDCP1) Is a Target for Radioligand Therapy in Castration-Resistant Prostate Cancer, including PSMA Null Disease.Clinical cancer research : an official journal of the American Association for Cancer Research · 2022Article
- Targeting CDCP1 gene transcription coactivated by BRD4 and CBP/p300 in castration-resistant prostate cancer.Oncogene · 2022Article
- Targeting a proteolytic neoepitope on CUB domain containing protein 1 (CDCP1) for RAS-driven cancers.The Journal of clinical investigation · 2022Article
- Substrate-biased activity-based probes identify proteases that cleave receptor CDCP1.Nature chemical biology · 2021Article
- Repurposing Tranexamic Acid as an Anticancer Agent.Frontiers in pharmacology · 2021Article
- Theranostic Targeting of CUB Domain Containing Protein 1 (CDCP1) in Pancreatic Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2020Article
- Anti-CDCP1 immuno-conjugates for detection and inhibition of ovarian cancer.Theranostics · 2020Article
- Effective targeting of intact and proteolysed CDCP1 for imaging and treatment of pancreatic ductal adenocarcinoma.Theranostics · 2020Article
- Kempopeptin C, a Novel Marine-Derived Serine Protease Inhibitor Targeting Invasive Breast Cancer.Marine drugs · 2017Article
- The role of type II transmembrane serine protease-mediated signaling in cancer.The FEBS journal · 2017Review
- SheddomeDB: the ectodomain shedding database for membrane-bound shed markers.BMC bioinformatics · 2017Review
- CDCP1 is a novel marker of the most aggressive human triple-negative breast cancers.Oncotarget · 2016Article
- Coupling an EML4-ALK-centric interactome with RNA interference identifies sensitizers to ALK inhibitors.Science signaling · 2016Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
CUB-domain-containing protein 1 (CDCP1) is an integral membrane glycoprotein with potential as a marker and therapeutic target for a number of cancers. Here we examine mechanisms regulating cellular processing of CDCP1. By analyzing cell lines exclusively passaged non-enzymatically and through use of a panel of protease inhibitors, we demonstrate that full-length 135 kDa CDCP1 is post-translationally processed in a range of cell lines by a mechanism involving serine protease activity, generating a C-terminal 70-kDa fragment. Immunopurification and N-terminal sequencing of this cell-retained fragment and detailed mutagenesis, show that proteolytic processing of CDCP1 occurs at two sites, Arg-368 and Lys-369. We show that the serine protease matriptase is an efficient, but not essential, cellular processor of CDCP1 at Arg-368. Importantly, we also demonstrate that proteolysis induces tyrosine phosphorylation of 70-kDa CDCP1 and recruitment of Src and PKCdelta to this fragment. In addition, Western blot and mass spectroscopy analyses show that an N-terminal 65-kDa CDCP1 ectodomain is shed intact from the cell surface. These data provide new insights into mechanisms regulating CDCP1 and suggest that the biological role of this protein and, potentially, its function in cancer, may be mediated by both 70-kDa cell retained and 65-kDa shed fragments, as well as the full-length 135-kDa protein.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.