Pub. Date : 2018 Nov
PMID : 29879417
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | OSBP binds, extracts and transfers sterols and phosphatidylinositol-4-phosphate (PI(4)P between liposomes, but the sequence of steps at the membrane surface leading to ligand removal is poorly characterized. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 2 | In this study, we used dual polarization interferometry (DPI), a label-free surface analytical technique, to characterize the interaction of recombinant, purified OSBP as it flows over immobilized dioleoyl-phosphatidylcholine (DOPC) bilayers containing PI(4)P, cholesterol or 25-hydroxycholesterol. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 3 | Kinetics of membrane interaction were analyzed for PI(4)P-binding and phosphorylation mutants of OSBP. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 4 | Wild-type OSBP demonstrated a distinctive association with immobilized DOPC bilayers containing 1-8 mol% PI(4)P that was characterized by initial saturable binding followed by desorption, indicative of PI(4)P extraction. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 5 | Wild-type OSBP demonstrated a distinctive association with immobilized DOPC bilayers containing 1-8 mol% PI(4)P that was characterized by initial saturable binding followed by desorption, indicative of PI(4)P extraction. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 6 | In support of this conclusion, an OSBP mutant with impaired binding and extraction of PI(4)P was stably absorbed to PI(4)P-containing membranes, while a pleckstrin homology domain mutant did not associate with PI(4)P-containing membranes. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 7 | In support of this conclusion, an OSBP mutant with impaired binding and extraction of PI(4)P was stably absorbed to PI(4)P-containing membranes, while a pleckstrin homology domain mutant did not associate with PI(4)P-containing membranes. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 8 | In support of this conclusion, an OSBP mutant with impaired binding and extraction of PI(4)P was stably absorbed to PI(4)P-containing membranes, while a pleckstrin homology domain mutant did not associate with PI(4)P-containing membranes. | pi(4)p | oxysterol binding protein | Homo sapiens |
| 9 | These real-time flow studies allow us to dissect the association of OSBP with PI(4)P into discrete components; initial recruitment to PI(4)P membranes by the PH domain, detection and extraction of PI(4)P, and desorption due to ligand depletion. | pi(4)p | oxysterol binding protein | Homo sapiens |