http://purl.uniprot.org/citations/20392696 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20392696 | http://www.w3.org/2000/01/rdf-schema#comment | "The Slo3 gene encodes a high conductance potassium channel, which is activated by both voltage and intracellular alkalinization. Slo3 is specifically expressed in mammalian sperm cells, where it gives rise to pH-dependent outwardly rectifying K(+) currents. Sperm Slo3 is the main current responsible for the capacitation-induced hyperpolarization, which is required for the ensuing acrosome reaction, an exocytotic process essential for fertilization. Here we show that in intact spermatozoa and in a heterologous expression system, the activation of Slo3 currents is regulated by phosphatidylinositol 4,5-bisphosphate (PIP(2)). Depletion of endogenous PIP(2) in inside-out macropatches from Xenopus oocytes inhibited heterologously expressed Slo3 currents. Whole-cell recordings of sperm Slo3 currents or of Slo3 channels co-expressed in Xenopus oocytes with epidermal growth factor receptor, demonstrated that stimulation by epidermal growth factor (EGF) could inhibit channel activity in a PIP(2)-dependent manner. High concentrations of PIP(2) in the patch pipette not only resulted in a strong increase in sperm Slo3 current density but also prevented the EGF-induced inhibition of this current. Mutation of positively charged residues involved in channel-PIP(2) interactions enhanced the EGF-induced inhibition of Slo3 currents. Overall, our results suggest that PIP(2) is an important regulator for Slo3 activation and that receptor-mediated hydrolysis of PIP(2) leads to inhibition of Slo3 currents both in native and heterologous expression systems."xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109.100156"xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/author | "Xia J."xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/author | "Ren D."xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/author | "Logothetis D.E."xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/author | "Tang Q.Y."xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/pages | "19259-19266"xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/title | "Phosphatidylinositol 4,5-bisphosphate activates Slo3 currents and its hydrolysis underlies the epidermal growth factor-induced current inhibition."xsd:string |
http://purl.uniprot.org/citations/20392696 | http://purl.uniprot.org/core/volume | "285"xsd:string |
http://purl.uniprot.org/citations/20392696 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20392696 |
http://purl.uniprot.org/citations/20392696 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20392696 |
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