| http://purl.uniprot.org/citations/12719424 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12719424 | http://www.w3.org/2000/01/rdf-schema#comment | "Several studies suggest that the Rh complex represents a major interaction site between the membrane lipid bilayer and the red cell skeleton, but little is known about the molecular basis of this interaction. We report here that ankyrin-R is capable of interacting directly with the C-terminal cytoplasmic domain of Rh and RhAG polypeptides. We first show that the primary defect of ankyrin-R in normoblastosis (nb/nb) spherocytosis mutant mice is associated with a sharp reduction of RhAG and Rh polypeptides. Secondly, our flow cytometric analysis of the Triton X-100 extractability of recombinant fusion proteins expressed in erythroleukemic cell lines suggests that the C-terminal cytoplasmic domains of Rh and RhAG are sufficient to mediate interaction with the erythroid membrane skeleton. Using the yeast two-hybrid system, we demonstrate a direct interaction between the cytoplasmic tails of Rh and RhAG and the second repeat domain (D2) of ankyrin-R. This finding is supported by the demonstration that the substitution of Asp-399 in the cytoplasmic tail of RhAG, a mutation associated with the deficiency of the Rh complex in one Rhnull patient, totally impaired interaction with domain D2 of ankyrin-R. These results identify the Rh/RhAG-ankyrin complex as a new interaction site between the red cell membrane and the spectrin-based skeleton, the disruption of which might result in the stomato-spherocytosis typical of Rhnull red cells."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m302816200"xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/author | "Colin Y."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/author | "Cartron J.P."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/author | "Gane P."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/author | "Le Van Kim C."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/author | "Mouro-Chanteloup I."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/author | "Birkenmeier C."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/author | "Nicolas V."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/pages | "25526-25533"xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/title | "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation."xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://purl.uniprot.org/core/volume | "278"xsd:string |
| http://purl.uniprot.org/citations/12719424 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12719424 |
| http://purl.uniprot.org/citations/12719424 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12719424 |
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| http://purl.uniprot.org/uniprot/#_A0A0R4J1N7-mappedCitation-12719424 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12719424 |
| http://purl.uniprot.org/uniprot/#_E9QNT8-mappedCitation-12719424 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12719424 |
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| http://purl.uniprot.org/uniprot/#_G3UY11-mappedCitation-12719424 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12719424 |