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Vol. 273, Issue 2, 720-728, January 9, 1998
From the Division of Regulation of Macromolecular Functions,
Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita,
Osaka 565, Japan
Necdin is a nuclear protein expressed in
virtually all postmitotic neurons, and ectopic expression of this
protein strongly suppresses the proliferation of NIH3T3 cells. Simian
virus 40 large T antigen targets both p53 and the retinoblastoma
protein (Rb) for cellular transformation. By analogy with the
interactions of the large T antigen with these nuclear growth
suppressors, we examined the ability of necdin to bind to the large T
antigen. Necdin was co-immunoprecipitated with the large T antigen from the nuclear extract of necdin cDNA-transfected COS-1 cells. Yeast two-hybrid and in vitro binding analyses revealed that
necdin bound to an amino-terminal region of the large T antigen, which encompasses the Rb-binding domain. Moreover, necdin bound to adenovirus E1A, another viral oncoprotein that forms a specific complex with Rb.
We then examined the ability of necdin to bind to the transcription factor E2F1, a cellular Rb-binding factor involved in cell-cycle progression. Intriguingly, necdin, like Rb, bound to a
carboxyl-terminal domain of E2F1, and repressed
E2F-dependent transactivation in vivo. In
addition, necdin suppressed the colony formation of Rb-deficient SAOS-2
osteosarcoma cells. These results suggest that necdin is a postmitotic
neuron-specific growth suppressor that is functionally similar to
Rb.
Necdin, A Postmitotic Neuron-specific Growth Suppressor,
Interacts with Viral Transforming Proteins and Cellular
Transcription Factor E2F1
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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