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J Biol Chem, Vol. 274, Issue 23, 16242-16248, June 4, 1999
From the Division of Regulation of Macromolecular Functions,
Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita,
Osaka 565-0871, Japan
Necdin is expressed in virtually all postmitotic
neurons, and ectopic expression of this protein suppresses cell
proliferation. Necdin, like the retinoblastoma protein, interacts with
cell cycle promoting proteins such as simian virus 40 large T antigen,
adenovirus E1A, and the transcription factor E2F1. Here we demonstrate
that necdin interacts with the tumor suppressor protein p53 as well. The yeast two-hybrid and in vitro binding analyses revealed
that necdin bound to a narrow region (amino acids 35-62) located
between the MDM2-binding site and the proline-rich region in the
amino-terminal domain of p53. The electrophoretic mobility shift assay
showed that necdin supershifted a complex between p53 and its binding DNA, implying that the p53-necdin complex is competent for DNA binding.
In p53-deficient osteosarcoma SAOS-2 cells, necdin markedly suppressed
p53-dependent activation of the p21/WAF promoter. Necdin and p53 inhibited cell growth in an additive manner as assessed by the
colony formation of SAOS-2 cells, suggesting that necdin does not
affect p53-mediated growth suppression. On the other hand, necdin
inhibited p53-induced apoptosis of osteosarcoma U2OS cells. Thus,
necdin can be a growth suppressor that targets p53 and modulates its
biological functions in postmitotic neurons.
Physical and Functional Interactions of Neuronal Growth
Suppressor Necdin with p53
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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