{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bavan S"],"funding":["Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["776-85"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3063728"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["79(4)"],"pubmed_abstract":["P2X ion channels have been functionally characterized from a range of eukaryotes. Although these receptors can be broadly classified into fast and slow desensitizing, the molecular mechanisms underlying current desensitization are not fully understood. Here, we describe the characterization of a P2X receptor from the cattle tick Boophilus microplus (BmP2X) displaying extremely slow current kinetics, little desensitization during ATP application, and marked rundown in current amplitude between sequential responses. ATP (EC(50), 67.1 μM) evoked concentration-dependent currents at BmP2X that were antagonized by suramin (IC(50), 4.8 μM) and potentiated by the antiparasitic drug amitraz. Ivermectin did not potentiate BmP2X currents, but the mutation M362L conferred ivermectin sensitivity. To in"],"journal":["Molecular pharmacology"],"pubmed_title":["The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus."],"pmcid":["PMC3063728"],"funding_grant_id":["WT081601MA"],"pubmed_authors":["Ennion SJ","Farmer L","Bavan S","Straub VA","Guerrero FD","Singh SK"],"additional_accession":[]},"is_claimable":false,"name":"The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus.","description":"P2X ion channels have been functionally characterized from a range of eukaryotes. Although these receptors can be broadly classified into fast and slow desensitizing, the molecular mechanisms underlying current desensitization are not fully understood. Here, we describe the characterization of a P2X receptor from the cattle tick Boophilus microplus (BmP2X) displaying extremely slow current kinetics, little desensitization during ATP application, and marked rundown in current amplitude between sequential responses. ATP (EC(50), 67.1 μM) evoked concentration-dependent currents at BmP2X that were antagonized by suramin (IC(50), 4.8 μM) and potentiated by the antiparasitic drug amitraz. Ivermectin did not potentiate BmP2X currents, but the mutation M362L conferred ivermectin sensitivity. To in","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Apr","modification":"2025-04-19T14:57:19.747Z","creation":"2019-03-27T00:40:00Z"},"accession":"S-EPMC3063728","cross_references":{"pubmed":["21212138"],"doi":["10.1124/mol.110.070037"]}}