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Article

A protein kinase-A recognition sequence is structurally linked to transformation by p59v-rel and cytoplasmic retention of p68c-rel.

Molecular and cellular biology - 1 Dec 1991

Mosialos G, Hamer P, Capobianco A J, Laursen R A, Gilmore T D

Abstract excerpt

The Rel family of proteins includes a number of proteins involved in transcriptional control, such as the retroviral oncoprotein v-Rel, c-Rel, the Drosophila melanogaster developmental protein Dorsal, and subunits of the transcription factor NF-kappa B. These proteins are related through a highly conserved domain of approximately 300 amino acids, called the Rel homology domain, that contains dimerization, DNA...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 1944267
DOI: 10.1128/mcb.11.12.5867-5877.1991
PMCID: PMC361736

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A protein kinase-A recognition sequence is structurally linked to transformation by p59v-rel and cytoplasmic retention of p68c-rel.PMID 1944267Read ↗

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Mutations within a conserved protein kinase A recognition sequence confer temperature-sensitive and partially defective activities onto mouse c-Rel.Semantic proximity Read ↗

Mutations of tumor necrosis factor alpha-responsive serine residues within the C-terminal transactivation domain of human transcription factor REL enhance its in vitro transforming ability.Semantic proximity Read ↗

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Mutant envelope residues confer a transactivation function onto N-terminal sequences of the v-Rel oncoprotein.Semantic proximity Read ↗

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The N-terminal env-derived amino acids of v-rel are required for full transforming activity.Semantic proximity Read ↗

Critical role of RelB serine 368 for dimerization and p100 stabilization.Semantic proximity Read ↗

An optimal range of transcription potency is necessary for efficient cell transformation by c-Rel to ensure optimal nuclear localization and gene-specific activation.Semantic proximity Read ↗

A conditional mutant of vRel containing sequences from the human estrogen receptor.Semantic proximity Read ↗

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