| http://purl.uniprot.org/citations/20961850 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20961850 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20961850 | http://www.w3.org/2000/01/rdf-schema#comment | "Members of the P(4) subfamily of P-type ATPases catalyze phospholipid transport and create membrane lipid asymmetry in late secretory and endocytic compartments. P-type ATPases usually pump small cations and the transport mechanism involved appears conserved throughout the family. How this mechanism is adapted to flip phospholipids remains to be established. P(4)-ATPases form heteromeric complexes with CDC50 proteins. Dissociation of the yeast P(4)-ATPase Drs2p from its binding partner Cdc50p disrupts catalytic activity (Lenoir, G., Williamson, P., Puts, C. F., and Holthuis, J. C. (2009) J. Biol. Chem. 284, 17956-17967), suggesting that CDC50 subunits play an intimate role in the mechanism of transport by P(4)-ATPases. The human genome encodes 14 P(4)-ATPases while only three human CDC50 homologues have been identified. This implies that each human CDC50 protein interacts with multiple P(4)-ATPases or, alternatively, that some human P(4)-ATPases function without a CDC50 binding partner. Here we show that human CDC50 proteins each bind multiple class-1 P(4)-ATPases, and that in all cases examined, association with a CDC50 subunit is required for P(4)-ATPase export from the ER. Moreover, we find that phosphorylation of the catalytically important Asp residue in human P(4)-ATPases ATP8B1 and ATP8B2 is critically dependent on their CDC50 subunit. These results indicate that CDC50 proteins are integral part of the P(4)-ATPase flippase machinery."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.139543"xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.139543"xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Devaux P.F."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Devaux P.F."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Hennrich H."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Hennrich H."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Holthuis J.C."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Holthuis J.C."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Lenoir G."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Lenoir G."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Bryde S."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Bryde S."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Verhulst P.M."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/author | "Verhulst P.M."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/pages | "40562-40572"xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/pages | "40562-40572"xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/title | "CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery."xsd:string |
| http://purl.uniprot.org/citations/20961850 | http://purl.uniprot.org/core/title | "CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery."xsd:string |