Annexin A4 interacts with the NF-kappa B p50 subunit and modulates NF-kappa B transcriptional activity in a Ca2+-dependent manner
- Authors
- Jeon, Young-Joo; Kim, Do-Hyung; Jung, Hyeyun; Chung, Sang J.; Chi, Seung-Wook; Cho, Sayeon; Lee, Sang Chul; Park, Byoung Chul; Park, Sung Goo; Bae, Kwang-Hee
- Issue Date
- Jul-2010
- Publisher
- SPRINGER BASEL AG
- Keywords
- Annexin; Annexin A4; Ca2+; Etoposide; NF-kappa B
- Citation
- CELLULAR AND MOLECULAR LIFE SCIENCES, v.67, no.13, pp 2271 - 2281
- Pages
- 11
- Journal Title
- CELLULAR AND MOLECULAR LIFE SCIENCES
- Volume
- 67
- Number
- 13
- Start Page
- 2271
- End Page
- 2281
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/22361
- DOI
- 10.1007/s00018-010-0331-9
- ISSN
- 1420-682X
1420-9071
- Abstract
- 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-kappa B through the Rel homology domain of p50. Furthermore, the interaction is markedly increased by elevated Ca2+ levels. NF-kappa B transcriptional activity assays demonstrated that ANXA4 suppresses NF-kappa B transcriptional activity in the resting state. Following treatment with TNF-alpha or PMA, ANXA4 also suppressed NF-kappa B 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-kappa B signaling pathway, depending on its interactions with p50 and the intracellular Ca2+ ion level.
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