Ribosomal protein S3 (rpS3) secreted from various cancer cells is N-linked glycosylated
- Authors
- Kim, YongJoong; Lee, Min Seon; Kim, Hag Dong; Kim, Joon
- Issue Date
- 6-12월-2016
- Publisher
- IMPACT JOURNALS LLC
- Keywords
- glycosylation; secretion; ribosomal protein S3; ribosome
- Citation
- ONCOTARGET, v.7, no.49, pp.80350 - 80362
- Indexed
- SCIE
SCOPUS
- Journal Title
- ONCOTARGET
- Volume
- 7
- Number
- 49
- Start Page
- 80350
- End Page
- 80362
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/86560
- DOI
- 10.18632/oncotarget.10180
- ISSN
- 1949-2553
- 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.
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