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Coactivator-Dependent Acetylation Stabilizes Members of the SREBP Family of Transcription Factors

Giandomenico, Valeria, Simonsson, Maria, Grünroos, Eva, Ericsson, Johan·2003·Molecular and Cellular Biology
DOI 10.1128/mcb.23.7.2587-2599.2003
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Abstract

Members of the SREBP family of transcription factors control cholesterol and lipid homeostasis and play important roles during adipocyte differentiation. The transcriptional activity of SREBPs is dependent on the coactivators p300 and CBP. We now present evidence that SREBPs are acetylated by the intrinsic acetyltransferase activity of p300 and CBP. In SREBP1a, the acetylated lysine residue resides in the DNA-binding domain of the protein. Coexpression with p300 dramatically increases the expression of both SREBP1a and SREBP2, and this effect is dependent on the acetyltransferase activity of p300, indicating that acetylation of SREBPs regulates their stability. Indeed, acetylation or mutation of the acetylated lysine residue in SREBP1a stabilizes the protein. We demonstrate that the acetylated residue in SREBP1a is also targeted by ubiquitination and that acetylation inhibits this process. Thus, our studies define acetylation-dependent stabilization of transcription factors as a novel mechanism for coactivators to regulate gene expression.

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  • SREBP-2 interacts with transcriptional co-activators CBP and p300 that acetylate SREBP-2 to stabilize its expression.

    “SREBP-2 also interacts with transcriptional co-activators, such as CBP and p300 that acetylate SREBP-2 to stabilize its expression29”

    From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [29]

Cites

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Sorted by citations

Authors
Giandomenico, V., Simonsson, M., Grünroos, E., & Ericsson, J.
Affiliations
Ludwig Institute for Cancer Research, S-751 24 Uppsala, Sweden
Venue
Molecular and Cellular Biology
Publisher
Informa UK Limited
Published
2003-04-01
Volume
23
Issue
7
Pages
2587-2599
ISSN
1098-5549
DOI
10.1128/mcb.23.7.2587-2599.2003
Cited by
205
References
3
Language
en
Licence
journals.asm.org/non-commercial-tdm-license (tdm)

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