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10.1080/19336950.2023.2200874 http://scihub22266oqcxt.onion/10.1080/19336950.2023.2200874 37040321!10761173!37040321     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=37040321&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       Channels+(Austin) 2023 ; 17 (1): 2200874 Nephropedia Template TP {{tp|p=37040321|t=2023. Effect of truncation on TRPM7 channel activity |pdf=|usr=}}{{37040321}} gab.com Text Effect of truncation on TRPM7 channel activity JO: Channels (Austin) http://www.kidney.de/pget.php?&tw=1&pmid=37040321 #FOAvip Transient receptor potential melastatin-like 7 (TRPM7) is a key player in various physiological and pathological processes. TRPM7 channel activity is regulated by different factors. The effects of cleavage of different domains on channel activity remain unknown. Here, we constructed several TRPM7 clones and explored the effects of truncating the mouse TRPM7 at different locations on the ion channel activity in two cell lines. We compared the clones' activity with the full-length TRPM7 and the native TRPM7 in transfected and untransfected cells. We also expressed fluorescently tagged truncated clones to examine their protein stability and membrane targeting. We found that truncating the kinase domain induced reduction in TRPM7 channel activity. Further truncations beyond the kinase (serine/threonine rich domain and/or coiled-coil domain) did not result in further reductions in channel activity. Two truncated clones lacking the TRP domain or the melastatin homology domain had a completely nonfunctional channel apparently due to disruption of protein stability. We identified the shortest structure of TRPM7 with measurable channel activity. We found that the truncated TRPM7 containing only S5 and S6 domains retained some channel activity. Adding the TRP domain to the S5-S6 resulted in a significant increase in channel activity. Finally, our analysis showed that TRPM7 outward currents are more sensitive to truncations than inward currents. Our data provide insights on the effects of truncating TRPM7 at different locations on the channel functions, highlighting the importance of different domains in impacting channel activity, protein stability, and/or membrane targeting. Twit Text FOAVip Effect of truncation on TRPM7 channel activity ????Channels (Austin) http://www.kidney.de/pget.php?&tw=1&pmid=37040321 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=37040321 #FOAvip English Wikipedia <ref>{{Cite pmid|37040321}}</ref> Effect of truncation on TRPM7 channel activity #MMPMID37040321 Xie Z; Abumaria N Channels (Austin) 2023[Dec]; 17 (1): 2200874 PMID37040321show ga Transient receptor potential melastatin-like 7 (TRPM7) is a key player in various physiological and pathological processes. TRPM7 channel activity is regulated by different factors. The effects of cleavage of different domains on channel activity remain unknown. Here, we constructed several TRPM7 clones and explored the effects of truncating the mouse TRPM7 at different locations on the ion channel activity in two cell lines. We compared the clones' activity with the full-length TRPM7 and the native TRPM7 in transfected and untransfected cells. We also expressed fluorescently tagged truncated clones to examine their protein stability and membrane targeting. We found that truncating the kinase domain induced reduction in TRPM7 channel activity. Further truncations beyond the kinase (serine/threonine rich domain and/or coiled-coil domain) did not result in further reductions in channel activity. Two truncated clones lacking the TRP domain or the melastatin homology domain had a completely nonfunctional channel apparently due to disruption of protein stability. We identified the shortest structure of TRPM7 with measurable channel activity. We found that the truncated TRPM7 containing only S5 and S6 domains retained some channel activity. Adding the TRP domain to the S5-S6 resulted in a significant increase in channel activity. Finally, our analysis showed that TRPM7 outward currents are more sensitive to truncations than inward currents. Our data provide insights on the effects of truncating TRPM7 at different locations on the channel functions, highlighting the importance of different domains in impacting channel activity, protein stability, and/or membrane targeting. |*TRPM Cation Channels/metabolism[MESH] |*Transient Receptor Potential Channels/metabolism[MESH] |Animals[MESH] |Cell Line[MESH] |Mice[MESH] |Protein Serine-Threonine Kinases/metabolism[MESH]Effect of truncation on TRPM7 channel activity (epmc).pdf DeepDyve Pubget Overpricing