SSRP1 functions as a co-activator of the transcriptional activator p63

Shelya X. Zeng; Mu Shui Dai; David M. Keller; Hua Lu

doi:10.1093/emboj/cdf540

SSRP1 functions as a co-activator of the transcriptional activator p63

Shelya X. Zeng, Mu Shui Dai, David M. Keller, Hua Lu

Molecular & Medical Genetics

Research output: Contribution to journal › Article › peer-review

75 Scopus citations

Abstract

The p53 homolog p63 is a transcriptional activator. Here, we describe the identification of an HMG1-like protein SSRP1 as a co-activator of p63. Over-expression of wild-type, but not deletion mutant, SSRP1 remarkably enhanced p63γ-dependent luciferase activity, G₁ arrest, apoptosis and expression of endogenous PIG3, p21^Waf1/cip1 and MDM2 in human p53-deficient lung carcinoma H1299 cells and mouse embryonic fibroblasts. Also, SSRP1 interacted to p63γ in vitro and in cells, and resided with p63γ at the p53-responsive DNA element sites of the cellular endogenous MDM2 and p21^Waf1/cip1 promoters. Moreover, N-terminus-deleted p63 (ΔN-p63) bound to neither SSRP1 nor its central domain in vitro. Accordingly, SSRP1 was unable to stimulate ΔN-p63-mediated residual luciferase activity and apoptosis in cells. Finally, the ectopic expression of the central p63-binding domain of SSRP1 inhibited p63-dependent transcription in cells. Thus, these results suggest that SSRP1 stimulates p63 activity by associating with this activator at the promoter.

Original language	English (US)
Pages (from-to)	5487-5497
Number of pages	11
Journal	EMBO Journal
Volume	21
Issue number	20
DOIs	https://doi.org/10.1093/emboj/cdf540
State	Published - Oct 15 2002

Keywords

Apoptosis and cell cycle
Co-activator
SSRP1
Transcription
p63

ASJC Scopus subject areas

Neuroscience(all)
Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

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title = "SSRP1 functions as a co-activator of the transcriptional activator p63",

abstract = "The p53 homolog p63 is a transcriptional activator. Here, we describe the identification of an HMG1-like protein SSRP1 as a co-activator of p63. Over-expression of wild-type, but not deletion mutant, SSRP1 remarkably enhanced p63γ-dependent luciferase activity, G1 arrest, apoptosis and expression of endogenous PIG3, p21Waf1/cip1 and MDM2 in human p53-deficient lung carcinoma H1299 cells and mouse embryonic fibroblasts. Also, SSRP1 interacted to p63γ in vitro and in cells, and resided with p63γ at the p53-responsive DNA element sites of the cellular endogenous MDM2 and p21Waf1/cip1 promoters. Moreover, N-terminus-deleted p63 (ΔN-p63) bound to neither SSRP1 nor its central domain in vitro. Accordingly, SSRP1 was unable to stimulate ΔN-p63-mediated residual luciferase activity and apoptosis in cells. Finally, the ectopic expression of the central p63-binding domain of SSRP1 inhibited p63-dependent transcription in cells. Thus, these results suggest that SSRP1 stimulates p63 activity by associating with this activator at the promoter.",

keywords = "Apoptosis and cell cycle, Co-activator, SSRP1, Transcription, p63",

author = "Zeng, {Shelya X.} and Dai, {Mu Shui} and Keller, {David M.} and Hua Lu",

year = "2002",

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AU - Zeng, Shelya X.

AU - Dai, Mu Shui

AU - Keller, David M.

AU - Lu, Hua

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AB - The p53 homolog p63 is a transcriptional activator. Here, we describe the identification of an HMG1-like protein SSRP1 as a co-activator of p63. Over-expression of wild-type, but not deletion mutant, SSRP1 remarkably enhanced p63γ-dependent luciferase activity, G1 arrest, apoptosis and expression of endogenous PIG3, p21Waf1/cip1 and MDM2 in human p53-deficient lung carcinoma H1299 cells and mouse embryonic fibroblasts. Also, SSRP1 interacted to p63γ in vitro and in cells, and resided with p63γ at the p53-responsive DNA element sites of the cellular endogenous MDM2 and p21Waf1/cip1 promoters. Moreover, N-terminus-deleted p63 (ΔN-p63) bound to neither SSRP1 nor its central domain in vitro. Accordingly, SSRP1 was unable to stimulate ΔN-p63-mediated residual luciferase activity and apoptosis in cells. Finally, the ectopic expression of the central p63-binding domain of SSRP1 inhibited p63-dependent transcription in cells. Thus, these results suggest that SSRP1 stimulates p63 activity by associating with this activator at the promoter.

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SSRP1 functions as a co-activator of the transcriptional activator p63

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