Identification of Complex-Formation between 2 Intracellular Tyrosine Kinase Substrates - Human C-Rel and the P105 Precursor of P50 Nf-Kappa-B

Neumann, M., Tsapos, K., Scheppler, J. A., Ross, J., Franza, B. R. (November 1992) Identification of Complex-Formation between 2 Intracellular Tyrosine Kinase Substrates - Human C-Rel and the P105 Precursor of P50 Nf-Kappa-B. Oncogene, 7 (11). pp. 2095-2104. ISSN 0950-9232

URL: http://www.ncbi.nlm.nih.gov/pubmed/1437141

Abstract

Immune complexes of the product of the c-rel protooncogene and of p105, the p50 NF-kappaB precursor, isolated from human T-lymphoblastoid cell lines are comprised of multiple proteins. Only p105 and human c-Rel (hc-Rel) are common to complexes precipitated with antiserum directed against either p105 or hc-Rel. Both proteins are inducible by phytohemagglutinin (PHA) and phorbol 12-myristate 13-acetate (PMA) and their subcellular distribution is affected by this induction. We demonstrate that the Rel immune complex contains a protein with a molecular weight in the 40 kDa range (p40) which apparently is exclusively cytoplasmic. We were not able to detect p40 in the p105 immune complex, though hc-Rel is present. This indicates that hc-Rel exists in different multi-protein complexes and fits a model of functional regulation mediated by differential protein-protein interaction. We also demonstrate considerable isoform diversity of both hc-Rel and p105. We show that this heterogeneity is, in part, the result of phosphorylation. Furthermore, we demonstrate that p105 and hc-Rel are tyrosine kinase substrates. This finding indicates a role for both proteins in intracellular signal transduction pathways which are modulated by modification of their phosphorylation status.

Item Type: Paper
Uncontrolled Keywords: HUMAN-IMMUNODEFICIENCY-VIRUS ENHANCER-BINDING-PROTEIN LONG TERMINAL REPEAT DNA-BINDING V-REL TRANSCRIPTION FACTORS CELLULAR PROTEINS STRAIN-T ACTIVATION CELLS
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > tyrosine kinase
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: November 1992
Date Deposited: 21 Sep 2015 15:22
Last Modified: 21 Sep 2015 15:22
URI: http://repository.cshl.edu/id/eprint/31847

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