Ribosomal protein S3 (rpS3) secreted from various cancer cells is N-linked glycosylated
DC Field | Value | Language |
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dc.contributor.author | Kim, YongJoong | - |
dc.contributor.author | Lee, Min Seon | - |
dc.contributor.author | Kim, Hag Dong | - |
dc.contributor.author | Kim, Joon | - |
dc.date.accessioned | 2021-09-03T15:52:30Z | - |
dc.date.available | 2021-09-03T15:52:30Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2016-12-06 | - |
dc.identifier.issn | 1949-2553 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/86560 | - |
dc.description.abstract | Ribosomal protein S3 (rpS3) is a 243 amino acid component of the 40S ribosomal small subunit. It has multiple roles in translation and extra-ribosomal functions like apoptosis and DNA repair. RpS3 is secreted only in cancer cell lines. Presently, mass spectrometry analysis revealed rpS3 to be glycosylated at the Asn165 residue. A point mutation at this residue decreased secretion of rpS3 in cancer cell lines. Secretion was also inhibited by the endoplasmic reticulum (ER)-Golgi transport inhibitor Brefeldin A and by Tunicamycin, an inhibitor of N-linked glycosylation. N-linked glycosylation of rpS3 was confirmed as necessary for rpS3 secretion into culture media via the ER-Golgi dependent pathway. RpS3 bound to Concanavalin A, a carbohydrate binding lectin protein, while treatment with peptide-N-glycosidase F shifted the secreted rpS3 to a lower molecular weight band. In addition, the N165G mutant of rpS3 displayed reduced secretion compared to the wild-type. An in vitro binding assay detected rpS3 homodimer formation via the N-terminal region (rpS3: 1-85) and a middle region (rpS3: 95-158). The results indicate that the Asn 165 residue of rpS3 is a critical site for N-linked glycosylation and passage through the ER-Golgi secretion pathway. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | IMPACT JOURNALS LLC | - |
dc.subject | GROWTH | - |
dc.subject | IDENTIFICATION | - |
dc.subject | MECHANISMS | - |
dc.subject | EXPRESSION | - |
dc.subject | INVASION | - |
dc.subject | DAMAGE | - |
dc.subject | GENES | - |
dc.subject | UBF | - |
dc.subject | P53 | - |
dc.title | Ribosomal protein S3 (rpS3) secreted from various cancer cells is N-linked glycosylated | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Joon | - |
dc.identifier.doi | 10.18632/oncotarget.10180 | - |
dc.identifier.scopusid | 2-s2.0-85001094040 | - |
dc.identifier.wosid | 000389877500024 | - |
dc.identifier.bibliographicCitation | ONCOTARGET, v.7, no.49, pp.80350 - 80362 | - |
dc.relation.isPartOf | ONCOTARGET | - |
dc.citation.title | ONCOTARGET | - |
dc.citation.volume | 7 | - |
dc.citation.number | 49 | - |
dc.citation.startPage | 80350 | - |
dc.citation.endPage | 80362 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Oncology | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Oncology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | INVASION | - |
dc.subject.keywordPlus | DAMAGE | - |
dc.subject.keywordPlus | GENES | - |
dc.subject.keywordPlus | UBF | - |
dc.subject.keywordPlus | P53 | - |
dc.subject.keywordAuthor | glycosylation | - |
dc.subject.keywordAuthor | secretion | - |
dc.subject.keywordAuthor | ribosomal protein S3 | - |
dc.subject.keywordAuthor | ribosome | - |
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