상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Annexin A4 interacts with the NF-kappaB p50 subunit and modulates NF-kappaB transcriptional activity in a Ca2+-dependent manner

Authors 

Y J JeonD H KimHyeyun JungSang Jeon ChungSeung-Wook ChiS ChoSang Chul LeeByoung Chul ParkSung Goo ParkKwang-Hee Bae

Publisher 

Springer Verlag (Germany)

Issue Date 

2010

Citation 

Cellular and Molecular Life Sciences, vol. 67, no. 13, pp. 2271-2281

Keywords 

AnnexinAnnexin A4Ca2+EtoposideNF-kB

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-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.

ISSN 

1420-682X

Link 

http://dx.doi.org/10.1007/s00018-010-0331-9

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)