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Discovery of small molecule inhibitors that effectively disrupt IQGAP1-Cdc42 interaction in breast cancer cells.
Sayedyahossein, Samar; Smith, Jessica; Barnaeva, Elena; Li, Zhigang; Choe, Jun; Ronzetti, Michael; Dextras, Christopher; Hu, Xin; Marugan, Juan; Southall, Noel; Baljinnyam, Bolormaa; Thines, Louise; Tran, Andy D; Ferrer, Marc; Sacks, David B.
Afiliação
  • Sayedyahossein S; Department of Laboratory Medicine, National Institutes of Health, Bethesda, MD, 20892, USA.
  • Smith J; Department of Physiology and Pharmacology, University of Western Ontario, London, ON, Canada.
  • Barnaeva E; Department of Laboratory Medicine, National Institutes of Health, Bethesda, MD, 20892, USA.
  • Li Z; Center for Scientific Review, National Institutes of Health, Bethesda, MD, USA.
  • Choe J; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Ronzetti M; Department of Laboratory Medicine, National Institutes of Health, Bethesda, MD, 20892, USA.
  • Dextras C; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Hu X; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Marugan J; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Southall N; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Baljinnyam B; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Thines L; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Tran AD; National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, MD, USA.
  • Ferrer M; Department of Laboratory Medicine, National Institutes of Health, Bethesda, MD, 20892, USA.
  • Sacks DB; Confocal Microscopy Core Facility, Laboratory of Cancer Biology and Genetics, NCI, National Institutes of Health, Rockville, MD, USA.
Sci Rep ; 12(1): 17372, 2022 10 17.
Article em En | MEDLINE | ID: mdl-36253497
The small GTPase Cdc42 is an integral component of the cytoskeleton, and its dysregulation leads to pathophysiological conditions, such as cancer. Binding of Cdc42 to the scaffold protein IQGAP1 stabilizes Cdc42 in its active form. The interaction between Cdc42 and IQGAP1 enhances migration and invasion of cancer cells. Disrupting this association could impair neoplastic progression and metastasis; however, no effective means to achieve this has been described. Here, we screened 78,500 compounds using a homogeneous time resolved fluorescence-based assay to identify small molecules that disrupt the binding of Cdc42 to IQGAP1. From the combined results of the validation assay and counter-screens, we selected 44 potent compounds for cell-based experiments. Immunoprecipitation and cell viability analysis rendered four lead compounds, namely NCGC00131308, NCGC00098561, MLS000332963 and NCGC00138812, three of which inhibited proliferation and migration of breast carcinoma cells. Microscale thermophoresis revealed that two compounds bind directly to Cdc42. One compound reduced the amount of active Cdc42 in cells and effectively impaired filopodia formation. Docking analysis provided plausible models of the compounds binding to the hydrophobic pocket adjacent to the GTP binding site of Cdc42. In conclusion, we identified small molecules that inhibit binding between Cdc42 and IQGAP1, which could potentially yield chemotherapeutic agents.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Neoplasias da Mama Limite: Female / Humans Idioma: En Revista: Sci Rep Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Neoplasias da Mama Limite: Female / Humans Idioma: En Revista: Sci Rep Ano de publicação: 2022 Tipo de documento: Article