| http://purl.uniprot.org/citations/10336610 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10336610 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10336610 | http://www.w3.org/2000/01/rdf-schema#comment | "In order to acquire an understanding of phospholipase C-delta3 (PLC-delta3) action on substrate localized in lipid membrane we have studied the binding of human recombinant PLC-delta3 to large, unilamellar phospholipid vesicles (LUVs). PLC-delta3 bound weakly to vesicles composed of phosphatidylcholine (PtdCho) or PtdCho plus phosphatidylethanolamine (PtdEtn) or phosphatidylinositol (PtdIns). The enzyme bound strongly to LUVs composed of PtdEtn + PtdCho and phosphatidylinositol 4,5-bisphosphate (PtdInsP2). The binding affinity (molar partition coefficient) of PLC-delta3 to PtdEtn + PtdCho + PtdInsP2 vesicles was 7.7 x 105 m-1. High binding of PLC-delta3 was also observed for LUVs composed of phosphatidic acid (PA). Binding of PLC-delta3 to phosphatidylserine (PtdSer) vesicles was less efficient. Calculated molar partition coefficient for binding of PLC-delta3 to PA and PtdSer vesicles was 1.6 x 104 m-1 and 9.4 x 102 m-1, respectively. Presence of PA in the LUVs containing PtdInsP2 considerably enhanced the binding of PLC-delta3 to the phospholipid membrane. Binding of PLC-delta3 to phospholipid vesicles was not dependent on Ca2+ presence. In the liposome assay PA caused a concentration-dependent increase in activity of PLC-delta3. The stimulatory effect of PA on PLC-delta3 was calcium-dependent. At Ca2+ concentrations lower than 1 microm, no effect of PA on the activity of PLC-delta3 was observed. PA enhanced PLC-delta3 activity by increasing the Vmax and lowering Km for PtdInsP2. As the mol fraction of PA increased from 0-40 mol% the enzyme Vmax increased 2.3-fold and Km decreased threefold. Based on the results presented, we assume that PA supports binding of PLC-delta3 to lipid membranes by interaction with the PH domain of the enzyme. The stimulatory effect of PA depends on calcium-dependent interaction with the C2 domain of PLC-delta3. We propose that binding of PLC-delta3 to PA may serve as a mechanism for dynamic membrane association and modulation of PLC-delta3 activity."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1327.1999.00388.x"xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1327.1999.00388.x"xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/author | "Pawelczyk T."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/author | "Pawelczyk T."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/author | "Matecki A."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/author | "Matecki A."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/pages | "291-298"xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/pages | "291-298"xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/title | "Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/title | "Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes."xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/volume | "262"xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://purl.uniprot.org/core/volume | "262"xsd:string |
| http://purl.uniprot.org/citations/10336610 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10336610 |
| http://purl.uniprot.org/citations/10336610 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10336610 |
| http://purl.uniprot.org/citations/10336610 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10336610 |
| http://purl.uniprot.org/citations/10336610 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10336610 |
| http://purl.uniprot.org/uniprot/Q8N3E9 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10336610 |
| http://purl.uniprot.org/uniprot/Q8N3E9#attribution-131BA76A7CE44A2FE213EF3B820F32BE | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10336610 |