N-linked glycosylation is essential for anti-tumor activities of KIAA1324 in gastric cancer
DC Field | Value | Language |
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dc.contributor.author | Yun, Rebecca | - |
dc.contributor.author | Hong, Eunji | - |
dc.contributor.author | Kim, Junil | - |
dc.contributor.author | Park, Bora | - |
dc.contributor.author | Kim, Staci Jakyong | - |
dc.contributor.author | Lee, Bona | - |
dc.contributor.author | Song, Yong Sang | - |
dc.contributor.author | Kim, Seong-Jin | - |
dc.contributor.author | Park, Sujin | - |
dc.contributor.author | Kang, Jin Muk | - |
dc.date.accessioned | 2023-10-06T01:40:02Z | - |
dc.date.available | 2023-10-06T01:40:02Z | - |
dc.date.created | 2023-10-05 | - |
dc.date.issued | 2023-08 | - |
dc.identifier.issn | 2041-4889 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/44359 | - |
dc.description.abstract | KIAA1324 is a transmembrane protein largely reported as a tumor suppressor and favorable prognosis marker in various cancers, including gastric cancer. In this study, we report the role of N-linked glycosylation in KIAA1324 as a functional post-translational modification (PTM). Loss of N-linked glycosylation eliminated the potential of KIAA1324 to suppress cancer cell proliferation and migration. Furthermore, we demonstrated that KIAA1324 undergoes fucosylation, a modification of the N-glycan mediated by fucosyltransferase, and inhibition of fucosylation also significantly suppressed KIAA1324-induced cell growth inhibition and apoptosis of gastric cancer cells. In addition, KIAA1324-mediated apoptosis and tumor regression were inhibited by the loss of N-linked glycosylation. RNA sequencing (RNAseq) analysis revealed that genes most relevant to the apoptosis and cell cycle arrest pathways were modulated by KIAA1324 with the N-linked glycosylation, and Gene Regulatory Network (GRN) analysis suggested novel targets of KIAA1324 for anti-tumor effects in the transcription level. The N-linked glycosylation blockade decreased protein stability through rapid proteasomal degradation. The non-glycosylated mutant also showed altered localization and lost apoptotic activity that inhibits the interaction between GRP78 and caspase 7. These data demonstrate that N-linked glycosylation of KIAA1324 is essential for the suppressive role of KIAA1324 protein in gastric cancer progression and indicates that KIAA1324 may have anti-tumor effects by targeting cancer-related genes with N-linked glycosylation. In conclusion, our study suggests the PTM of KIAA1324 including N-linked glycosylation and fucosylation is a necessary factor to consider for cancer prognosis and therapy improvement. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | SPRINGERNATURE | - |
dc.relation.isPartOf | CELL DEATH & DISEASE | - |
dc.title | N-linked glycosylation is essential for anti-tumor activities of KIAA1324 in gastric cancer | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/s41419-023-06083-6 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | CELL DEATH & DISEASE, v.14, no.8 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 001053844900005 | - |
dc.identifier.scopusid | 2-s2.0-85168429615 | - |
dc.citation.number | 8 | - |
dc.citation.title | CELL DEATH & DISEASE | - |
dc.citation.volume | 14 | - |
dc.contributor.affiliatedAuthor | Kim, Junil | - |
dc.identifier.url | https://www.nature.com/articles/s41419-023-06083-6 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | Y | - |
dc.subject.keywordPlus | SET ENRICHMENT ANALYSIS | - |
dc.subject.keywordPlus | PROGRESSION | - |
dc.subject.keywordPlus | GRP78 | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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