Co-relation with novel phosphorylation sites of I kappa B alpha and necroptosis in breast cancer cells
DC Field | Value | Language |
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dc.contributor.author | Choi, Sung Hoon | - |
dc.contributor.author | Yoon, Hee-Sub | - |
dc.contributor.author | Yoo, Shin-Ae | - |
dc.contributor.author | Yun, Sung Ho | - |
dc.contributor.author | Park, Joo-Hee | - |
dc.contributor.author | Han, Eun Hee | - |
dc.contributor.author | Chi, Sung-Gil | - |
dc.contributor.author | Chung, Young-Ho | - |
dc.date.accessioned | 2021-11-19T15:40:25Z | - |
dc.date.available | 2021-11-19T15:40:25Z | - |
dc.date.created | 2021-08-30 | - |
dc.date.issued | 2021-05-24 | - |
dc.identifier.issn | 1471-2407 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/128009 | - |
dc.description.abstract | BackgroundPhosphorylation of NF-kappaB inhibitor alpha (I kappa B alpha) is key to regulation of NF-kappa B transcription factor activity in the cell. Several sites of I kappa B alpha phosphorylation by members of the I kappa B kinase family have been identified, but phosphorylation of the protein by other kinases remains poorly understood. We investigated a new phosphorylation site on I kappa B alpha and identified its biological function in breast cancer cells.MethodsPreviously, we observed that aurora kinase (AURK) binds I kappa B alpha in the cell. To identify the domains of I kappa B alpha essential for phosphorylation by AURK, we performed kinase assays with a series of I kappa B alpha truncation mutants. AURK significantly promoted activation of I kappa B alpha at serine 32 but not serine 36; by contrast, I kappa B kinase (IKK) family proteins activated both of these residues. We also confirmed phosphorylation of I kappa B alpha by matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/TOF MS) and nano-liquid chromatography hybrid quadrupole orbitrap mass spectrometer (nanoLC-MS/MS; Q-Exactive).ResultsWe identified two novel sites of serine phosphorylation, S63 and S262. Alanine substitution of S63 and S262 (S63A and S262A) of I kappa B alpha inhibited proliferation and suppressed p65 transcription activity. In addition, S63A and/or S262A of I kappa B alpha regulated apoptotic and necroptotic effects in breast cancer cells.ConclusionsPhosphorylation of I kappa B alpha by AURK at novel sites is related to the apoptosis and necroptosis pathways in breast cancer cells. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | BMC | - |
dc.subject | ACTIVATION | - |
dc.subject | NECROSIS | - |
dc.subject | AURORA | - |
dc.subject | DEGRADATION | - |
dc.subject | APOPTOSIS | - |
dc.subject | KINASES | - |
dc.subject | PATHWAY | - |
dc.subject | FAMILY | - |
dc.subject | GROWTH | - |
dc.title | Co-relation with novel phosphorylation sites of I kappa B alpha and necroptosis in breast cancer cells | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chi, Sung-Gil | - |
dc.identifier.doi | 10.1186/s12885-021-08304-7 | - |
dc.identifier.scopusid | 2-s2.0-85106940380 | - |
dc.identifier.wosid | 000657731100004 | - |
dc.identifier.bibliographicCitation | BMC CANCER, v.21, no.1 | - |
dc.relation.isPartOf | BMC CANCER | - |
dc.citation.title | BMC CANCER | - |
dc.citation.volume | 21 | - |
dc.citation.number | 1 | - |
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.journalWebOfScienceCategory | Oncology | - |
dc.subject.keywordPlus | NECROSIS | - |
dc.subject.keywordPlus | AURORA | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | APOPTOSIS | - |
dc.subject.keywordPlus | KINASES | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordAuthor | Breast cancer | - |
dc.subject.keywordAuthor | I kappa B alpha | - |
dc.subject.keywordAuthor | New phospho-site | - |
dc.subject.keywordAuthor | Necroptosis | - |
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