Regulation of the RelA (p65) transactivation domain

John M. O'Shea; Neil D. Perkins

doi:10.1042/BST0360603

Regulation of the RelA (p65) transactivation domain

John M. O'Shea, Neil D. Perkins

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

64 Citations (Scopus)

Abstract

The RelA (p65) NF-kappaB (nuclear factor kappaB) subunit contains an extremely active C-terminal transcriptional activation domain, required for its cellular function. In the present article, we review our knowledge of this domain, its modifications and its known interacting proteins. Moreover, we discuss how analysis of its evolutionary conservation reveals distinct subdomains and conserved residues that might give insights into its regulation and function.

Original language	English
Pages (from-to)	603-8
Number of pages	6
Journal	Biochemical Society Transactions
Volume	36
Issue number	Pt 4
DOIs	https://doi.org/10.1042/BST0360603
Publication status	Published - Aug 2008

Keywords

Amino Acid Motifs
Animals
Gene Expression Regulation
Humans
Ligases
Protein Binding
Transcriptional Activation

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10.1042/BST0360603

http://www.biochemsoctrans.org/bst/036/bst0360603.htm

Cite this

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abstract = "The RelA (p65) NF-kappaB (nuclear factor kappaB) subunit contains an extremely active C-terminal transcriptional activation domain, required for its cellular function. In the present article, we review our knowledge of this domain, its modifications and its known interacting proteins. Moreover, we discuss how analysis of its evolutionary conservation reveals distinct subdomains and conserved residues that might give insights into its regulation and function.",

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KW - Amino Acid Motifs

KW - Animals

KW - Gene Expression Regulation

KW - Humans

KW - Ligases

KW - Protein Binding

KW - Transcriptional Activation

U2 - 10.1042/BST0360603

DO - 10.1042/BST0360603

M3 - Article

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EP - 608

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - Pt 4

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Regulation of the RelA (p65) transactivation domain

Abstract

Keywords

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