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Article

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

Oncogene - 1 Mar 1993

Mosialos G, Gilmore T D

Abstract excerpt

The avian retroviral oncoprotein v-Rel and its cellular homolog c-Rel are members of a family of related site-specific DNA-binding proteins. Towards the carboxy-terminal end of the highly conserved Rel homology (RH) domain in the majority of Rel proteins, there is a consensus recognition sequence for protein kinase A (PK-A). We have investigated the importance of this sequence (Arg-Arg-Pro-Ser) for several...

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PMID: 8437855

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v-Rel and c-Rel are differentially affected by mutations at a consensus protein kinase recognition sequence.PMID 8437855Read ↗

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

Discreet mutations from c-Rel to v-Rel alter kappaB DNA recognition, IkappaBalpha binding, and dimerization: implications for v-Rel oncogenicity.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 ↗

Multiple mutations contribute to the oncogenicity of the retroviral oncoprotein v-Rel.Semantic proximity Read ↗

NF-κB c-Rel Dictates the Inflammatory Threshold by Acting as a Transcriptional RepressorSemantic 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 ↗

In vivo evolution of c-rel oncogenic potential.Semantic proximity Read ↗

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

Interaction of the v-Rel oncoprotein with cellular transcription factor Sp1.Semantic proximity Read ↗

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

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