Premium
A20, an inhibitor of cell death, self‐associates by its zinc finger domain
Author(s) -
De Valck Dirk,
Heyninck Karen,
Van Criekinge Wim,
Contreras Roland,
Beyaert Rudi,
Fiers Walter
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00283-9
Subject(s) - zinc finger , ring finger domain , microbiology and biotechnology , programmed cell death , yeast , apoptosis , chemistry , protein–protein interaction , zinc , gene , biology , biochemistry , transcription factor , organic chemistry
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.