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

Young-Joo Jeon1, Do-Hyung Kim, Hyeyun Jung

  • 1Medical Proteomics Research Center, KRIBB, Daejeon, 305-806, Republic of Korea.

Cellular and Molecular Life Sciences : CMLS
|March 19, 2010
PubMed

Insights

Annexin A4 (ANXA4) interacts with NF-kappaB, modulating its activity and nuclear translocation. This interaction, influenced by calcium levels, enhances cellular resistance to apoptosis.

Area of Science:

  • Cellular Biology
  • Molecular Signaling

Background:

  • Annexin A4 (ANXA4) was previously identified as a potential substrate for caspase-3.
  • Understanding ANXA4's cellular roles necessitates identifying its interacting partners.

Purpose of the Study:

  • To identify proteins interacting with ANXA4.
  • To elucidate the functional consequences of ANXA4-protein interactions on cellular signaling pathways.

Main Methods:

  • Proteomic studies were employed to identify ANXA4-interacting proteins.
  • NF-kappaB transcriptional activity assays were conducted.
  • Confocal microscopy was used to track protein localization.

Main Results:

  • ANXA4 was found to interact with p105 and specifically with NF-kappaB via the p50 subunit's Rel homology domain.
  • The ANXA4-p50 interaction is calcium-dependent and suppresses NF-kappaB activity under resting and stimulated conditions (TNF-alpha, PMA).
  • ANXA4 translocates to the nucleus with p50, conferring increased resistance to etoposide-induced apoptosis.

Conclusions:

  • ANXA4 differentially modulates the NF-kappaB signaling pathway.
  • The modulation is dependent on ANXA4's interaction with p50 and intracellular calcium levels.
  • ANXA4 plays a role in cellular protection against apoptotic stimuli.

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