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https://doi.org/10.1038/cddis.2015.266
| Title: | RILP suppresses invasion of breast cancer cells by modulating the activity of RalA through interaction with RalGDS | Authors: | Wang, Z Zhou, Y Hu, X Chen, W Lin, X Sun, L Xu, X Hong, W Wang, T |
Keywords: | guanine nucleotide exchange factor mitogen activated protein kinase protein protein kinase B rab7 interacting lysosomal protein rala protein short hairpin RNA unclassified drug guanine nucleotide exchange factor protein binding Ral protein RALA protein, human RILP protein, human signal transducing adaptor protein actin filament amino terminal sequence Article breast cancer breast cancer cell line cell behavior assay cell invasion cell lysate cell proliferation controlled study cytoplasm endosome enzyme phosphorylation gene overexpression gene silencing human human cell immunofluorescence microscopy immunoprecipitation migration inhibition nonhuman priority journal reverse transcription polymerase chain reaction RNA interference signal transduction transwell assay Western blotting wound healing migration assay breast tumor cell motion chemistry female MCF-7 cell line metabolism pathology physiology protein domain protein transport tumor invasion Adaptor Proteins, Signal Transducing Breast Neoplasms Cell Movement Cell Proliferation Endosomes Female Humans MAP Kinase Signaling System MCF-7 Cells Neoplasm Invasiveness Protein Binding Protein Interaction Domains and Motifs Protein Transport ral GTP-Binding Proteins ral Guanine Nucleotide Exchange Factor |
Issue Date: | 2015 | Publisher: | Nature Publishing Group | Citation: | Wang, Z, Zhou, Y, Hu, X, Chen, W, Lin, X, Sun, L, Xu, X, Hong, W, Wang, T (2015). RILP suppresses invasion of breast cancer cells by modulating the activity of RalA through interaction with RalGDS. Cell Death and Disease 6 (10) : e1923. ScholarBank@NUS Repository. https://doi.org/10.1038/cddis.2015.266 | Rights: | Attribution 4.0 International | Abstract: | RILP (Rab7-interacting lysosomal protein) is a key regulator for late endosomal/lysosomal trafficking, and probably a tumor suppressor in prostate cancer. However, the role of RILP in other cancers and the underlying mechanism for RILP in regulating the invasion of cancer cells remain to be investigated. In this study, we showed that overexpression of RILP in breast cancer cells inhibits the migration and invasion, whereas the depletion of RILP by RNAi-mediated knockdown promotes the migration and invasion. We identified RalGDS (Ral guanine nucleotide dissociation stimulator) as a novel interacting partner for RILP, and truncation analysis revealed the N-terminal region of RILP is responsible for interacting with the guanine nucleotide exchange factor (GEF) domain of RalGDS. Immunofluorescence microscopy revealed that RalGDS can be recruited to the late endosomal compartments by RILP. Further investigations indicated that the overexpression of RILP inhibits the activity of RalA, a downstream target of RalGDS. Our data suggest that RILP suppresses the invasion of breast cancer cells by interacting with RalGDS to inhibit its GEF activity for RalA. © 2015 Macmillan Publishers Limited . | Source Title: | Cell Death and Disease | URI: | https://scholarbank.nus.edu.sg/handle/10635/180432 | ISSN: | 2041-4889 | DOI: | 10.1038/cddis.2015.266 | Rights: | Attribution 4.0 International |
| Appears in Collections: | Elements Staff Publications |
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