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- Title
Annexin A4 interacts with the NF-κB p50 subunit and modulates NF-κB transcriptional activity in a Ca<sup>2+</sup>-dependent manner.
- Authors
Young-Joo Jeon; Do-Hyung Kim; Hyeyun Jung; Chun, Sang J.; Seung-Wook Chi; Sayeon Cho; Sang Chul Lee; Byoung Chul Park; Sung Goo Park; Kwang-Hee Bae
- 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-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.
- Subjects
ANNEXINS; HOMOLOGY (Biology); ETOPOSIDE; CALCIUM; NF-kappa B
- Publication
Cellular & Molecular Life Sciences, 2010, Vol 67, Issue 13, p2271
- ISSN
1420-682X
- Publication type
Article
- DOI
10.1007/s00018-010-0331-9