| http://purl.uniprot.org/citations/15699139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15699139 | http://www.w3.org/2000/01/rdf-schema#comment | "MTJ-1 associates with a glucose-regulated protein of Mr approximately 78,000(GRP78) in the endoplasmic reticulum and modulates GRP78 activity as a chaperone. GRP78 also exists on the cell surface membrane, where it is associated with a number of functions. MHC class I Ags on the cell surface are complexed to GRP78. GRP78 also serves as the receptor for alpha2-macroglobulin-dependent signaling and for uptake of certain pathogenic viruses. The means by which GRP78, lacking a transmembrane domain, can fulfill such functions is unclear. In this study we have examined the question of whether MTJ-1, a transmembrane protein, is involved in the translocation of GRP78 to the cell surface. MTJ-1 and GRP78 coimmunoprecipitated from macrophage plasma membrane lysates. Silencing of MTJ-1 gene expression greatly reduced MTJ-1 mRNA and protein levels, but also abolished cell surface localization of GRP78. Consequently, binding of the activated and receptor-recognized form of alpha2-macroglobulin to macrophages was greatly reduced, and activated and receptor-recognized form of alpha2-macroglobulin-induced calcium signaling was abolished in these cells. In conclusion, we show that in addition to assisting the chaperone GRP78 in protein quality control in the endoplasmic reticulum, MTJ-1 is essential for transport of GRP78 to the cell surface, which serves a number of functions in immune regulation and signal transduction."xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.174.4.2092"xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/author | "Pizzo S.V."xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/author | "Gonzalez-Gronow M."xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/author | "Misra U.K."xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/author | "Gawdi G."xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/pages | "2092-2097"xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/title | "The role of MTJ-1 in cell surface translocation of GRP78, a receptor for alpha 2-macroglobulin-dependent signaling."xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://purl.uniprot.org/core/volume | "174"xsd:string |
| http://purl.uniprot.org/citations/15699139 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15699139 |
| http://purl.uniprot.org/citations/15699139 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15699139 |
| http://purl.uniprot.org/uniprot/#_A0A0A6YXF5-mappedCitation-15699139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15699139 |
| http://purl.uniprot.org/uniprot/#_F7C8U2-mappedCitation-15699139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15699139 |
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| http://purl.uniprot.org/uniprot/#_Q3TI47-mappedCitation-15699139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15699139 |
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