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- Annexin A4 interacts with the NF-kappaB p50 subunit and modulates NF-kappaB transcriptional activity in a Ca2+-dependent manner
- Young Joo Jeon; D H Kim; Hyeyun Jung; Sang Jeon Chung; Seung-Wook Chi; S Cho; Sang Chul Lee; Byoung Chul Park; Sung Goo Park; Kwang-Hee Bae
- Bibliographic Citation
- Cellular and Molecular Life Sciences, vol. 67, no. 13, pp. 2271-2281
- Publication Year
- 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-kB through the Rel homology domain of p50. Furthermore, the interaction is markedly increased by elevated Ca2+ levels. NF-kB transcriptional activity assays demonstrated that ANXA4 suppresses NF-kB transcriptional activity in the resting state. Following treatment with TNF-α or PMA, ANXA4 also suppressed NF-kB 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-kB signaling pathway, depending on its interactions with p50 and the intracellular Ca2+ ion level.
- AnnexinAnnexin A4Ca2+EtoposideNF-kB
- Appears in Collections:
- Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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