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10.1101/2023.01.19.524765 http://scihub22266oqcxt.onion/10.1101/2023.01.19.524765 36711628!9882303!36711628     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=36711628&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       bioRxiv 2023 ; ? (?): ? Nephropedia Template TP {{tp|p=36711628|t=2023. Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15 |pdf=|usr=}}{{36711628}} gab.com Text Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15 JO: bioRxiv http://www.kidney.de/pget.php?&tw=1&pmid=36711628 #FOAvip Cystathionine-beta-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They promote efflux of Mg (2+) ions on their own or uptake of divalent cations when coupled to the transient receptor potential ion channel subfamily M member 7 (TRPM7). Recently, ADP-ribosylation factor-like GTPase 15 (ARL15) has been identified as CNNM binding partner and an inhibitor of divalent cation influx by TRPM7. Here, we characterize ARL15 as a GTP-binding protein and demonstrate that it binds the CNNM CBS-pair domain with low micromolar affinity. The crystal structure of the complex between ARL15 GTPase domain and CNNM2 CBS-pair domain reveals the molecular determinants of the interaction and allowed the identification of mutations in ARL15 and CNNM2 mutations that abrogate binding. Loss of CNNM binding prevented ARL15 suppression of TRPM7 channel activity in support of previous reports that the proteins function as a ternary complex. Binding experiments with phosphatase of regenerating liver 2 (PRL2 or PTP4A2) revealed that ARL15 and PRLs compete for binding CNNM, suggesting antagonistic regulation of divalent cation transport by the two proteins. Twit Text FOAVip Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15 ????bioRxiv http://www.kidney.de/pget.php?&tw=1&pmid=36711628 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=36711628 #FOAvip English Wikipedia <ref>{{Cite pmid|36711628}}</ref> Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15 #MMPMID36711628 Mahbub L; Kozlov G; Zong P; Tetteh S; Nethramangalath T; Knorn C; Jiang J; Shahsavan A; Lee E; Yue L; Runnels LW; Gehring K bioRxiv 2023[Jan]; ? (?): ? PMID36711628show ga Cystathionine-beta-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They promote efflux of Mg (2+) ions on their own or uptake of divalent cations when coupled to the transient receptor potential ion channel subfamily M member 7 (TRPM7). Recently, ADP-ribosylation factor-like GTPase 15 (ARL15) has been identified as CNNM binding partner and an inhibitor of divalent cation influx by TRPM7. Here, we characterize ARL15 as a GTP-binding protein and demonstrate that it binds the CNNM CBS-pair domain with low micromolar affinity. The crystal structure of the complex between ARL15 GTPase domain and CNNM2 CBS-pair domain reveals the molecular determinants of the interaction and allowed the identification of mutations in ARL15 and CNNM2 mutations that abrogate binding. Loss of CNNM binding prevented ARL15 suppression of TRPM7 channel activity in support of previous reports that the proteins function as a ternary complex. Binding experiments with phosphatase of regenerating liver 2 (PRL2 or PTP4A2) revealed that ARL15 and PRLs compete for binding CNNM, suggesting antagonistic regulation of divalent cation transport by the two proteins. ?Structural insights into regulation of TRPM7 divalent cation uptake by(epmc).pdf DeepDyve Pubget Overpricing