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We began analyzing https://link.springer.com/article/10.1007/s00018-010-0331-9, but it redirected us to https://link.springer.com/article/10.1007/s00018-010-0331-9. The analysis below is for the second page.

Title[redir]:
Annexin A4 interacts with the NF-κB p50 subunit and modulates NF-κB transcriptional activity in a Ca2+-dependent manner | Cellular and Molecular Life Sciences
Description:
Previously, we identified annexin A4 (ANXA4) as a candidate substrate of caspase-3. Proteomic studies were performed to identify interacting proteins with a view to determining the roles of ANXA4. ANXA4 was found to interact with the p105. Subsequent studies revealed that ANXA4 interacts with NF-κB through the Rel homology domain of p50. Furthermore, the interaction is markedly increased by elevated Ca2+ levels. NF-κB transcriptional activity assays demonstrated that ANXA4 suppresses NF-κB transcriptional activity in the resting state. Following treatment with TNF-α or PMA, ANXA4 also suppressed NF-κB transcriptional activity, which was upregulated significantly early after etoposide treatment. This difference may be due to the intracellular Ca2+ level. Additionally, ANXA4 translocates to the nucleus together with p50, and imparts greater resistance to apoptotic stimulation by etoposide. Our results collectively indicate that ANXA4 differentially modulates the NF-κB signaling pathway, depending on its interactions with p50 and the intracellular Ca2+ ion level.

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Keywords {🔍}

article, cas, google, scholar, pubmed, park, nfκb, annexin, kim, lee, cell, bae, cancer, anxa, protein, research, cho, transcription, annexins, privacy, cookies, content, life, transcriptional, activity, access, cells, mol, sci, proteomics, analysis, information, publish, search, jeon, sang, chung, chul, signaling, factor, res, expression, clin, human, rev, science, regulation, kang, korea, data,

Topics {✒️}

matrix-assisted laser desorption/ionization-time transcription factor nf-κb nf-κb transcription factor nf-kb transcription factors month download article/chapter nf-κb signaling pathway nf-κb signaling system nf-κb p50 subunit 2d-dige saturation labeling nuclear factor-κb sung goo park kwang-hee bae upstream element-binding protein-1 ca2+-dependent manner nf-κb complexes annexin a4 interacts ca2+-dependent phospholipid identified annexin a4 calcium-dependent binding related subjects full article pdf nemo nuclear export intracellular ca2+ level privacy choices/manage cookies korea research council calcium-dependent regulation linking ca2+ signalling nf-κb elevated ca2+ levels young min kim pro-adhesion state kh domain subunit ah young lee anxa4 differentially modulates annexin a4 ethanol-induced augmentation annexin iv expression arachidonic acid binding ribosomal protein s3 chromatin granule binding article jeon european economic area protein expression profiling helicobacter pylori infection rat c6 glioma evolutionary conserved mediators dimensional gel electrophoresis hbx-transgenic mice lar tyrosine phosphatase 3t3–l1 preadipocytes

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         description:Previously, we identified annexin A4 (ANXA4) as a candidate substrate of caspase-3. Proteomic studies were performed to identify interacting proteins with a view to determining the roles of ANXA4. ANXA4 was found to interact with the p105. Subsequent studies revealed that ANXA4 interacts with NF-κB through the Rel homology domain of p50. Furthermore, the interaction is markedly increased by elevated Ca2+ levels. NF-κB transcriptional activity assays demonstrated that ANXA4 suppresses NF-κB transcriptional activity in the resting state. Following treatment with TNF-α or PMA, ANXA4 also suppressed NF-κB transcriptional activity, which was upregulated significantly early after etoposide treatment. This difference may be due to the intracellular Ca2+ level. Additionally, ANXA4 translocates to the nucleus together with p50, and imparts greater resistance to apoptotic stimulation by etoposide. Our results collectively indicate that ANXA4 differentially modulates the NF-κB signaling pathway, depending on its interactions with p50 and the intracellular Ca2+ ion level.
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