| http://purl.uniprot.org/citations/18940794 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18940794 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18940794 | http://www.w3.org/2000/01/rdf-schema#comment | "Copper metabolism Murr1 domain 1 (COMMD1) is a 21-kDa protein involved in copper export from the liver, NF-kappaB signaling, HIV infection, and sodium transport. The precise function of COMMD and the mechanism through which COMMD1 performs its multiple roles are not understood. Recombinant COMMD1 is a soluble protein, yet in cells COMMD1 is largely seen as targeted to cellular membranes. Using co-localization with organelle markers and cell fractionation, we determined that COMMD1 is located in the vesicles of the endocytic pathway, whereas little COMMD1 is detected in either the trans-Golgi network or lysosomes. The mechanism of COMMD1 recruitment to cell membranes was investigated using lipid-spotted arrays and liposomes. COMMD1 specifically binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) in the absence of other proteins and does not bind structural lipids; the phosphorylation of PtdIns at position 4 is essential for COMMD1 binding. Proteolytic sensitivity and molecular modeling experiments identified two distinct domains in the structure of COMMD1. The C-terminal domain appears sufficient for lipid binding, because both the full-length and C-terminal domain proteins bind to PtdIns(4,5)P2. In native conditions, endogenous COMMD1 forms large oligomeric complexes both in the cytosol and at the membrane; interaction with PtdIns(4,5)P2 increases the stability of oligomers. Altogether, our results suggest that COMMD1 is a scaffold protein in a distinct sub-compartment of endocytic pathway and offer first clues to its role as a regulator of structurally unrelated membrane transporters."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m804766200"xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m804766200"xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Burkhead J.L."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Burkhead J.L."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Lutsenko S."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Lutsenko S."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Shinde U."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Shinde U."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Haddock G."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Haddock G."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Morgan C.T."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/author | "Morgan C.T."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/pages | "696-707"xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/pages | "696-707"xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/title | "COMMD1 forms oligomeric complexes targeted to the endocytic membranes via specific interactions with phosphatidylinositol 4,5-bisphosphate."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/title | "COMMD1 forms oligomeric complexes targeted to the endocytic membranes via specific interactions with phosphatidylinositol 4,5-bisphosphate."xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/volume | "284"xsd:string |
| http://purl.uniprot.org/citations/18940794 | http://purl.uniprot.org/core/volume | "284"xsd:string |