CUB domain-containing protein 1 and the epidermal growth factor receptor cooperate to induce cell detachment.

Background: While localized malignancies often respond to available therapies, most disseminated cancers are refractory. Novel approaches, therefore, are needed for the treatment of metastatic disease. CUB domain-containing protein1 (CDCP1) plays an important role in metastasis and drug resistance;...

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Publicado en:Breast Cancer Research Vol. 18; pp. 1 - 18
Autores principales: Law, Mary E., Ferreira, Renan B., Davis, Bradley J., Higgins, Paul J., Jae-Sung Kim, Castellano, Ronald K., Sixue Chen, Luesch, Hendrik, Law, Brian K., Kim, Jae-Sung, Chen, Sixue
Formato: research Journal Article
Publicado: BioMed Central 8/5/2016
Acceso en línea:Ver este registro en EBSCOhost
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        14655411
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      jtl: Breast Cancer Research
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      dt: 8/5/2016
      vid: 18
      pid: 24147
      pub: BioMed Central
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        NLM27495374
        117302832
        10.1186/s13058-016-0741-1
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        atl: CUB domain-containing protein 1 and the epidermal growth factor receptor cooperate to induce cell detachment.
      aug:
        au:
          Law, Mary E.
          Ferreira, Renan B.
          Davis, Bradley J.
          Higgins, Paul J.
          Jae-Sung Kim
          Castellano, Ronald K.
          Sixue Chen
          Luesch, Hendrik
          Law, Brian K.
          Kim, Jae-Sung
          Chen, Sixue
        affil: Department of Pharmacology and Therapeutics, University of Florida, Acad. Res. Bldg., Room R5-210, 1200 Newell Drive, P.O. Box 100267, Gainesville, FL 32610, USA
      sug:
        subj:
          Proteins Physiology
          Antigens, Surface Physiology
          Epidermal Growth Factors Metabolism
          Cell Adhesion Molecules Physiology
          Female
          Glycoproteins Metabolism
          Transferases Metabolism
          Cell Physiology
          Breast Neoplasms
          Cell Line, Tumor Pathology
          Neoplasm Metastasis
          Biological Transport
          Cell Line, Tumor Metabolism
          Funding Source
          Human
          Female
      ab: Background: While localized malignancies often respond to available therapies, most disseminated cancers are refractory. Novel approaches, therefore, are needed for the treatment of metastatic disease. CUB domain-containing protein1 (CDCP1) plays an important role in metastasis and drug resistance; the mechanism however, is poorly understood.Methods: Breast cancer cell lines were engineered to stably express EGFR, CDCP1 or phosphorylation site mutants of CDCP1. These cell lines were used for immunoblot analysis or affinity purification followed by immunoblot analysis to assess protein phosphorylation and/or protein complex formation with CDCP1. Kinase activity was evaluated using phosphorylation site-specific antibodies and immunoblot analysis in in vitro kinase assays. Protein band excision and mass spectrometry was utilized to further identify proteins complexed with CDCP1 or ΔCDCP1, which is a mimetic of the cleaved form of CDCP1. Cell detachment was assessed using cell counting.Results: This paper reports that CDCP1 forms ternary protein complexes with Src and EGFR, facilitating Src activation and Src-dependent EGFR transactivation. Importantly, we have discovered that a class of compounds termed Disulfide bond Disrupting Agents (DDAs) blocks CDCP1/EGFR/Src ternary complex formation and downstream signaling. CDCP1 and EGFR cooperate to induce detachment of breast cancer cells from the substratum and to disrupt adherens junctions. Analysis of CDCP1-containing complexes using proteomics techniques reveals that CDCP1 associates with several proteins involved in cell adhesion, including adherens junction and desmosomal cadherins, and cytoskeletal elements.Conclusions: Together, these results suggest that CDCP1 may facilitate loss of adhesion by promoting activation of EGFR and Src at sites of cell-cell and cell-substratum contact.
      pubtype: Academic Journal
      doctype:
        research
        Journal Article
      ougenre: Article
    language: English
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