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

doi:10.1128/mcb.11.12.5867-5877.1991

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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...

Topics

Amino Acid Sequence
Animals
Base Sequence
Blotting, Western
Cell Transformation, Neoplastic
Chickens
Cytoplasm
DNA
Molecular Sequence Data
Mutation
Oncogene Proteins v-rel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Kinases

Proto-Oncogene Proteins

Proto-Oncogene Proteins c-rel

Retroviridae Proteins, Oncogenic

Substrate Specificity

Transcription, Genetic

Trypsin

Source

Open in PubMed Open full text

Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1944267-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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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 ↗

v-Rel and c-Rel are differentially affected by mutations at a consensus protein kinase recognition sequence.Semantic proximity Read ↗

Differences in kappaB DNA-binding properties of v-Rel and c-Rel are the result of oncogenic mutations in three distinct functional regions of the Rel protein.Semantic proximity Read ↗

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 ↗

Mutations in the DNA-binding and dimerization domains of v-Rel are responsible for altered kappa B DNA-binding complexes in transformed cells.Semantic proximity Read ↗

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

Transformation by the vRel oncoprotein requires sequences carboxy-terminal to the Rel homology domain.Semantic proximity Read ↗

RelA Ser276 Phosphorylation-Coupled Lys310 Acetylation Controls Transcriptional Elongation of Inflammatory Cytokines in Respiratory Syncytial Virus InfectionSemantic proximity Read ↗

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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