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10.1016/j.redox.2017.08.013 http://scihub22266oqcxt.onion/10.1016/j.redox.2017.08.013 C5582718!5582718 !28869833     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28869833 &cmd=llinks): Failed to open stream: HTTP request failed! 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Yap promotes hepatocellular carcinoma metastasis and mobilization via governing cofilin/F-actin/lamellipodium axis by regulation of JNK/Bnip3/SERCA/CaMKII pathways |pdf=|usr=}}{{28869833 }} gab.com Text Yap promotes hepatocellular carcinoma metastasis and mobilization via governing cofilin/F-actin/lamellipodium axis by regulation of JNK/Bnip3/SERCA/CaMKII pathways JO: Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=28869833 #FOAvip Despite the increasingly important role of Hippo-Yap in hepatocellular carcinoma (HCC) development and progression, little insight is available at the time regarding the specifics interaction of Yap and cancer cells migration. Here, we identified the mechanism by which tumor-intrinsic Yap deletion resulted in HCC migratory inhibition. Yap was greatly upregulated in HCC and its expression promoted the cells migration. Functional studies found that knockdown of Yap induced JNK phosphorylation which closely bound to the Bnip3 promoter and contributed to Bnip3 expression. Higher Bnip3 employed excessive mitophagy leading to mitochondrial dysfunction and ATP shortage. The insufficient ATP inactivated SERCA and consequently triggered intracellular calcium overload. As the consequence of calcium oscillation, Ca/calmodulin-dependent protein kinases II (CaMKII) was signaled and subsequently inhibited cofilin activity via phosphorylated modification. The phosphorylated cofilin failed to manipulate F-actin polymerization and lamellipodium formation, resulting into the impairment of lamellipodium-based migration. Collectively, our results identified Hippo-Yap as the tumor promoter in hepatocellular carcinoma that mediated via activation of cofilin/F-actin/lamellipodium axis by limiting JNK-Bnip3-SERCA-CaMKII pathways, with potential application to HCC therapy involving cancer metastasis. Twit Text FOAVip Yap promotes hepatocellular carcinoma metastasis and mobilization via governing cofilin/F-actin/lamellipodium axis by regulation of JNK/Bnip3/SERCA/CaMKII pathways ????Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=28869833 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28869833 #FOAvip English Wikipedia <ref>{{Cite pmid|28869833 }}</ref> Yap promotes hepatocellular carcinoma metastasis and mobilization via governing cofilin/F-actin/lamellipodium axis by regulation of JNK/Bnip3/SERCA/CaMKII pathways #MMPMID28869833 Shi C ; Cai Y ; Li Y ; Li Y ; Hu N ; Ma S ; Hu S ; Zhu P ; Wang W ; Zhou H Redox Biol 2018[Apr]; 14 (ä): 59-71 PMID28869833 show ga Despite the increasingly important role of Hippo-Yap in hepatocellular carcinoma (HCC) development and progression, little insight is available at the time regarding the specifics interaction of Yap and cancer cells migration. Here, we identified the mechanism by which tumor-intrinsic Yap deletion resulted in HCC migratory inhibition. Yap was greatly upregulated in HCC and its expression promoted the cells migration. Functional studies found that knockdown of Yap induced JNK phosphorylation which closely bound to the Bnip3 promoter and contributed to Bnip3 expression. Higher Bnip3 employed excessive mitophagy leading to mitochondrial dysfunction and ATP shortage. The insufficient ATP inactivated SERCA and consequently triggered intracellular calcium overload. As the consequence of calcium oscillation, Ca/calmodulin-dependent protein kinases II (CaMKII) was signaled and subsequently inhibited cofilin activity via phosphorylated modification. The phosphorylated cofilin failed to manipulate F-actin polymerization and lamellipodium formation, resulting into the impairment of lamellipodium-based migration. Collectively, our results identified Hippo-Yap as the tumor promoter in hepatocellular carcinoma that mediated via activation of cofilin/F-actin/lamellipodium axis by limiting JNK-Bnip3-SERCA-CaMKII pathways, with potential application to HCC therapy involving cancer metastasis. |*Signal Transduction [MESH] |Actin Depolymerizing Factors/*metabolism [MESH] |Actins/*metabolism [MESH] |Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism [MESH] |Calcium/metabolism [MESH] |Carcinoma, Hepatocellular/metabolism/*pathology [MESH] |Cell Cycle Proteins [MESH] |Cell Line, Tumor [MESH] |Cell Movement [MESH] |Energy Metabolism [MESH] |Hep G2 Cells [MESH] |Humans [MESH] |JNK Mitogen-Activated Protein Kinases/metabolism [MESH] |Liver Neoplasms/metabolism/*pathology [MESH] |Membrane Proteins/metabolism [MESH] |Nuclear Proteins/antagonists & inhibitors/genetics/*metabolism [MESH] |Phosphorylation [MESH] |Proto-Oncogene Proteins/metabolism [MESH] |RNA Interference [MESH] |RNA, Small Interfering/metabolism [MESH] |Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism [MESH] |Transcription Factors/antagonists & inhibitors/genetics/*metabolism [MESH]Yap promotes hepatocellular carcinoma metastasis and mobilization via (epmc).pdf DeepDyve Pubget Overpricing