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10.1074/jbc.M115.705863 http://scihub22266oqcxt.onion/10.1074/jbc.M115.705863 26969161!4865918!26969161     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26969161&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2016 ; 291 (20): 10716-25 Nephropedia Template TP {{tp|p=26969161|t=2016. Inhibition of PRL-2 CNNM3 Protein Complex Formation Decreases Breast Cancer Proliferation and Tumor Growth |pdf=|usr=}}{{26969161}} gab.com Text Inhibition of PRL-2 CNNM3 Protein Complex Formation Decreases Breast Cancer Proliferation and Tumor Growth JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26969161 #FOAvip The oncogenic phosphatase of regenerating liver 2 (PRL-2) has been shown to regulate intracellular magnesium levels by forming a complex through an extended amino acid loop present in the Bateman module of the CNNM3 magnesium transporter. Here we identified highly conserved residues located on this amino acid loop critical for the binding with PRL-2. A single point mutation (D426A) of one of those critical amino acids was found to completely disrupt PRL-2.human Cyclin M 3 (CNNM3) complex formation. Whole-cell voltage clamping revealed that expression of CNNM3 influenced the surface current, whereas overexpression of the binding mutant had no effect, indicating that the binding of PRL-2 to CNNM3 is important for the activity of the complex. Interestingly, overexpression of the CNNM3 D426A-binding mutant in cancer cells decreased their ability to proliferate under magnesium-deprived situations and under anchorage-independent growth conditions, demonstrating a PRL-2.CNNM3 complex-dependent oncogenic advantage in a more stringent environment. We further confirmed the importance of this complex in vivo using an orthotopic xenograft breast cancer model. Finally, because molecular modeling showed that the Asp-426 side chain in CNNM3 buries into the catalytic cavity of PRL-2, we showed that a PRL inhibitor could abrogate complex formation, resulting in a decrease in proliferation of human breast cancer cells. In summary, we provide evidence that this fundamental regulatory aspect of PRL-2 in cancer cells could potentially lead to broadly applicable and innovative therapeutic avenues. Twit Text FOAVip Inhibition of PRL-2 CNNM3 Protein Complex Formation Decreases Breast Cancer Proliferation and Tumor Growth ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26969161 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26969161 #FOAvip English Wikipedia <ref>{{Cite pmid|26969161}}</ref> Inhibition of PRL-2 CNNM3 Protein Complex Formation Decreases Breast Cancer Proliferation and Tumor Growth #MMPMID26969161 Kostantin E; Hardy S; Valinsky WC; Kompatscher A; de Baaij JH; Zolotarov Y; Landry M; Uetani N; Martinez-Cruz LA; Hoenderop JG; Shrier A; Tremblay ML J Biol Chem 2016[May]; 291 (20): 10716-25 PMID26969161show ga The oncogenic phosphatase of regenerating liver 2 (PRL-2) has been shown to regulate intracellular magnesium levels by forming a complex through an extended amino acid loop present in the Bateman module of the CNNM3 magnesium transporter. Here we identified highly conserved residues located on this amino acid loop critical for the binding with PRL-2. A single point mutation (D426A) of one of those critical amino acids was found to completely disrupt PRL-2.human Cyclin M 3 (CNNM3) complex formation. Whole-cell voltage clamping revealed that expression of CNNM3 influenced the surface current, whereas overexpression of the binding mutant had no effect, indicating that the binding of PRL-2 to CNNM3 is important for the activity of the complex. Interestingly, overexpression of the CNNM3 D426A-binding mutant in cancer cells decreased their ability to proliferate under magnesium-deprived situations and under anchorage-independent growth conditions, demonstrating a PRL-2.CNNM3 complex-dependent oncogenic advantage in a more stringent environment. We further confirmed the importance of this complex in vivo using an orthotopic xenograft breast cancer model. Finally, because molecular modeling showed that the Asp-426 side chain in CNNM3 buries into the catalytic cavity of PRL-2, we showed that a PRL inhibitor could abrogate complex formation, resulting in a decrease in proliferation of human breast cancer cells. In summary, we provide evidence that this fundamental regulatory aspect of PRL-2 in cancer cells could potentially lead to broadly applicable and innovative therapeutic avenues. |Animals[MESH] |Breast Neoplasms/*metabolism/pathology/*therapy[MESH] |Cell Line, Tumor[MESH] |Cell Proliferation/drug effects[MESH] |Conserved Sequence[MESH] |Cyclins/*antagonists & inhibitors/chemistry/genetics[MESH] |Female[MESH] |Humans[MESH] |Mice[MESH] |Mice, Nude[MESH] |Models, Molecular[MESH] |Mutant Proteins/genetics/metabolism[MESH] |Point Mutation[MESH] |Protein Interaction Domains and Motifs/drug effects[MESH] |Protein Tyrosine Phosphatases/*antagonists & inhibitors/chemistry/genetics[MESH] |Pyridones/pharmacology[MESH] |Tumor Stem Cell Assay[MESH]Inhibition of PRL-2 CNNM3 Protein Complex Formation Decreases Breast C(epmc).pdf DeepDyve Pubget Overpricing