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10.1242/jcs.141689 http://scihub22266oqcxt.onion/10.1242/jcs.141689 C4074264!4074264 !24659799     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24659799 &cmd=llinks): Failed to open stream: HTTP request failed! 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Rab5 is required in metastatic cancer cells for Caveolin-1-enhanced Rac1 activation, migration and invasion |pdf=|usr=}}{{24659799 }} gab.com Text Rab5 is required in metastatic cancer cells for Caveolin-1-enhanced Rac1 activation, migration and invasion JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=24659799 #FOAvip Rab5 is a small GTPase that regulates early endosome trafficking and other cellular processes, including cell adhesion and migration. Specifically, Rab5 promotes Rac1 activation and cancer cell migration, but little is known about the upstream regulators of Rab5. We have previously shown that the scaffolding protein Caveolin-1 (CAV1) promotes Rac1 activation and migration of cancer cells. Here, we hypothesized that CAV1 stimulates Rab5 activation, leading to increased Rac1 activity and cell migration. Expression of CAV1 in B16-F10 mouse melanoma and HT-29(US) human colon adenocarcinoma cells increased the GTP loading of Rab5, whereas shRNA-mediated targeting of endogenous CAV1 in MDA-MB-231 breast cancer cells decreased Rab5-GTP levels. Accordingly, shRNA-mediated downregulation of Rab5 decreased CAV1-mediated Rac1 activation, cell migration and invasion in B16-F10 and HT-29(US) cells. Expression of CAV1 was accompanied by increased recruitment of Tiam1, a Rac1 guanine nucleotide exchange factor (GEF), to Rab5-positive early endosomes. Using the inhibitor NSC23766, Tiam1 was shown to be required for Rac1 activation and cell migration induced by CAV1 and Rab5. Mechanistically, we provide evidence implicating p85? (also known as PIK3R1), a Rab5 GTPase-activating protein (GAP), in CAV1-dependent effects, by showing that CAV1 recruits p85?, precluding p85?-mediated Rab5 inactivation and increasing cell migration. In summary, these studies identify a novel CAV1-Rab5-Rac1 signaling axis, whereby CAV1 prevents Rab5 inactivation, leading to increased Rac1 activity and enhanced tumor cell migration and invasion. Twit Text FOAVip Rab5 is required in metastatic cancer cells for Caveolin-1-enhanced Rac1 activation, migration and invasion ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=24659799 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24659799 #FOAvip English Wikipedia <ref>{{Cite pmid|24659799 }}</ref> Rab5 is required in metastatic cancer cells for Caveolin-1-enhanced Rac1 activation, migration and invasion #MMPMID24659799 Díaz J ; Mendoza P ; Ortiz R ; Díaz N ; Leyton L ; Stupack D ; Quest AF ; Torres VA J Cell Sci 2014[Jun]; 127 (Pt 11 ): 2401-6 PMID24659799 show ga Rab5 is a small GTPase that regulates early endosome trafficking and other cellular processes, including cell adhesion and migration. Specifically, Rab5 promotes Rac1 activation and cancer cell migration, but little is known about the upstream regulators of Rab5. We have previously shown that the scaffolding protein Caveolin-1 (CAV1) promotes Rac1 activation and migration of cancer cells. Here, we hypothesized that CAV1 stimulates Rab5 activation, leading to increased Rac1 activity and cell migration. Expression of CAV1 in B16-F10 mouse melanoma and HT-29(US) human colon adenocarcinoma cells increased the GTP loading of Rab5, whereas shRNA-mediated targeting of endogenous CAV1 in MDA-MB-231 breast cancer cells decreased Rab5-GTP levels. Accordingly, shRNA-mediated downregulation of Rab5 decreased CAV1-mediated Rac1 activation, cell migration and invasion in B16-F10 and HT-29(US) cells. Expression of CAV1 was accompanied by increased recruitment of Tiam1, a Rac1 guanine nucleotide exchange factor (GEF), to Rab5-positive early endosomes. Using the inhibitor NSC23766, Tiam1 was shown to be required for Rac1 activation and cell migration induced by CAV1 and Rab5. Mechanistically, we provide evidence implicating p85? (also known as PIK3R1), a Rab5 GTPase-activating protein (GAP), in CAV1-dependent effects, by showing that CAV1 recruits p85?, precluding p85?-mediated Rab5 inactivation and increasing cell migration. In summary, these studies identify a novel CAV1-Rab5-Rac1 signaling axis, whereby CAV1 prevents Rab5 inactivation, leading to increased Rac1 activity and enhanced tumor cell migration and invasion. |Aminoquinolines/pharmacology [MESH] |Animals [MESH] |Caveolin 1/genetics/*metabolism [MESH] |Cell Movement/drug effects/genetics [MESH] |Class Ia Phosphatidylinositol 3-Kinase [MESH] |DNA-Binding Proteins/metabolism [MESH] |Guanine Nucleotide Exchange Factors/metabolism [MESH] |HT29 Cells [MESH] |Humans [MESH] |Melanoma, Experimental [MESH] |Mice [MESH] |Neoplasm Invasiveness/genetics [MESH] |Neoplasm Metastasis/genetics [MESH] |Phosphatidylinositol 3-Kinases/metabolism [MESH] |Pyrimidines/pharmacology [MESH] |RNA, Small Interfering/genetics [MESH] |Signal Transduction/drug effects/genetics [MESH] |T-Lymphoma Invasion and Metastasis-inducing Protein 1 [MESH] |Transcription Factors/metabolism [MESH] |rab5 GTP-Binding Proteins/genetics/*metabolism [MESH]Rab5 is required in metastatic cancer cells for Caveolin-1-enhanced Ra(epmc).pdf DeepDyve Pubget Overpricing