{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Demaree IS"],"funding":["NIA NIH HHS","NHLBI NIH HHS","NINDS NIH HHS","NIAMS NIH HHS","NIGMS NIH HHS","NIH HHS"],"pagination":["2019"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11640535"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(23)"],"pubmed_abstract":["<h4>Background</h4>TRPC5 proteins form plasma membrane cation channels and are expressed in the nervous and cardiovascular systems. TRPC5 activation leads to cell depolarization and increases neuronal excitability, whereas a homologous TRPC1 inhibits TRPC5 function via heteromerization. The mechanism underlying the inhibitory effect of TRPC1 in TRPC5/TRPC1 heteromers remains unknown.<h4>Methods</h4>We used electrophysiological techniques to examine the roles of subunit stoichiometry and positively charged luminal residues of TRPC1 on TRPC5/TRPC1 function. We also performed molecular dynamics simulations.<h4>Results</h4>We found that increasing the relative amount of TRPC1 in TRPC5/TRPC1 heteromers reduced histamine-induced cation influx through the heteromeric channels. Consistently, hista"],"journal":["Cells"],"pubmed_title":["Effects of TRPC1's Lysines on Heteromeric TRPC5-TRPC1 Channel Function."],"pmcid":["PMC11640535"],"funding_grant_id":["R01 AG075132","R01 GM111639","HL083381, HL115140, NS102415, AG075132","R01 HL115140","R01 GM115844","R01 AR083130","R01 NS102415","R01 HL083381"],"pubmed_authors":["Hoang QQ","Demaree IS","Obukhov AG","Tennessen K","White FA","Kumar S"],"additional_accession":[]},"is_claimable":false,"name":"Effects of TRPC1's Lysines on Heteromeric TRPC5-TRPC1 Channel Function.","description":"<h4>Background</h4>TRPC5 proteins form plasma membrane cation channels and are expressed in the nervous and cardiovascular systems. TRPC5 activation leads to cell depolarization and increases neuronal excitability, whereas a homologous TRPC1 inhibits TRPC5 function via heteromerization. The mechanism underlying the inhibitory effect of TRPC1 in TRPC5/TRPC1 heteromers remains unknown.<h4>Methods</h4>We used electrophysiological techniques to examine the roles of subunit stoichiometry and positively charged luminal residues of TRPC1 on TRPC5/TRPC1 function. We also performed molecular dynamics simulations.<h4>Results</h4>We found that increasing the relative amount of TRPC1 in TRPC5/TRPC1 heteromers reduced histamine-induced cation influx through the heteromeric channels. Consistently, hista","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-04-23T03:25:49.53Z","creation":"2025-04-04T01:54:20.975Z"},"accession":"S-EPMC11640535","cross_references":{"pubmed":["39682767"],"doi":["10.3390/cells13232019"]}}