| http://purl.uniprot.org/citations/23347038 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23347038 | http://www.w3.org/2000/01/rdf-schema#comment | "The M6P (mannose 6-phosphate)/IGF2R (insulin-like growth factor II receptor) interacts with a variety of factors that impinge on tumour invasion and metastasis. It has been shown that expression of wild-type M6P/IGF2R reduces the tumorigenic and invasive properties of receptor-deficient SCC-VII squamous cell carcinoma cells. We have now used mutant forms of M6P/IGF2R to assess the relevance of the different ligand-binding sites of the receptor for its biological activities in this cellular system. The results of the present study demonstrate that M6P/IGF2R does not require a functional binding site for insulin-like growth factor II for inhibition of anchorage-independent growth and matrix invasion by SCC-VII cells. In contrast, the simultaneous mutation of both M6P-binding sites is sufficient to impair all cellular functions of the receptor tested. These findings highlight that the interaction between M6P/IGF2R and M6P-modified ligands is not only important for intracellular accumulation of lysosomal enzymes and formation of dense lysosomes, but is also crucial for the ability of the receptor to suppress SCC-VII growth and invasion. The present study also shows that some of the biological activities of M6P/IGF2R in SCC-VII cells strongly depend on a functional M6P-binding site within domain 3, thus providing further evidence for the non-redundant cellular functions of the individual carbohydrate-binding domains of the receptor."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20121422"xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/author | "Mach L."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/author | "Hehenberger E."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/author | "Karayel E."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/author | "Probst O.C."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/author | "Puxbaum V."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/author | "Nimmerfall E."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/author | "Schida N."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/pages | "91-99"xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/title | "The mannose 6-phosphate-binding sites of M6P/IGF2R determine its capacity to suppress matrix invasion by squamous cell carcinoma cells."xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://purl.uniprot.org/core/volume | "451"xsd:string |
| http://purl.uniprot.org/citations/23347038 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23347038 |
| http://purl.uniprot.org/citations/23347038 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23347038 |
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| http://purl.uniprot.org/uniprot/#_Q13661-mappedCitation-23347038 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23347038 |
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