A20, an inhibitor of cell death, self-associates by its zinc finger domain

A20 is a primary response gene which is induced after monocyte adherence or cytokine stimulation of a variety of cells. The A20 protein belongs to a novel class of Cys 2/Cys 2 zinc finger proteins, and has been characterized as an inhibitor of both apoptotic and necrotic cell death. In order to clar...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1996-04, Vol.384 (1), p.61-64
Main Authors: De Valck, Dirk, Heyninck, Karen, Van Criekinge, Wim, Contreras, Roland, Beyaert, Rudi, Fiers, Walter
Format: Article
Language:English
Subjects:
Apoptosis
Base Sequence
Binding Sites
Breast Neoplasms
Cell Death
Cell Line
Cloning, Molecular
Cysteine
DNA Primers
DNA-Binding Proteins
Female
Gene Expression - drug effects
Humans
Intracellular Signaling Peptides and Proteins
Molecular Sequence Data
Necrosis
Nuclear Proteins
Polymerase Chain Reaction
Protein Binding
Protein Biosynthesis
Protein-protein interaction
Proteins - isolation & purification
Proteins - metabolism
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - isolation & purification
Recombinant Proteins - pharmacology
Self-association
Tumor Cells, Cultured
Tumor necrosis factor
Tumor Necrosis Factor alpha-Induced Protein 3
Tumor Necrosis Factor-alpha - pharmacology
Zinc finger protein
Zinc Fingers
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A20 is a primary response gene which is induced after monocyte adherence or cytokine stimulation of a variety of cells. The A20 protein belongs to a novel class of Cys 2/Cys 2 zinc finger proteins, and has been characterized as an inhibitor of both apoptotic and necrotic cell death. In order to clarify its molecular mechanism of action, we used the yeast-based-two-hybrid system to screen for A20-associated proteins. Here we report that A20 is able to self-associate, and demonstrate that the latter interaction is mediated by its zinc finger domain.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(96)00283-9