TY - JOUR
T1 - COMMD proteins, a novel family of structural and functional homologs of MURR1
AU - Burstein, Ezra
AU - Hoberg, Jamie E.
AU - Wilkinson, Amanda S.
AU - Rumble, Julie M.
AU - Csomos, Rebecca A.
AU - Komarck, Christine M.
AU - Maine, Gabriel N.
AU - Wilkinson, John C.
AU - Mayo, Marty W.
AU - Duckett, Colin S.
PY - 2005/6/10
Y1 - 2005/6/10
N2 - MURR1 is a multifunctional protein that inhibits nuclear factor κB (NF-κB), a transcription factor with pleiotropic functions affecting innate and adaptive immunity, apoptosis, cell cycle regulation, and oncogenesis. Here we report the discovery of a new family of proteins with homology to MURR1. These proteins form multimeric complexes and were identified in a biochemical screen for MURR1-associated factors. The family is defined by the presence of a conserved and unique motif termed the COMM (copper metabolism gene MURR1) domain, which functions as an interface for protein-protein interactions. Like MURR1, several of these factors also associate with and inhibit NF-κB. The proteins designated as COMMD or COMM domain containing 1-10 are extensively conserved in multicellular eukaryotic organisms and define a novel family of structural and functional homologs of MURR1. The prototype of this family, MURR1/COMMD1, suppresses NF-κB not by affecting nuclear translocation or binding of NF-κB to cognate motifs; rather, it functions in the nucleus by affecting the association of NF-κB with chromatin.
AB - MURR1 is a multifunctional protein that inhibits nuclear factor κB (NF-κB), a transcription factor with pleiotropic functions affecting innate and adaptive immunity, apoptosis, cell cycle regulation, and oncogenesis. Here we report the discovery of a new family of proteins with homology to MURR1. These proteins form multimeric complexes and were identified in a biochemical screen for MURR1-associated factors. The family is defined by the presence of a conserved and unique motif termed the COMM (copper metabolism gene MURR1) domain, which functions as an interface for protein-protein interactions. Like MURR1, several of these factors also associate with and inhibit NF-κB. The proteins designated as COMMD or COMM domain containing 1-10 are extensively conserved in multicellular eukaryotic organisms and define a novel family of structural and functional homologs of MURR1. The prototype of this family, MURR1/COMMD1, suppresses NF-κB not by affecting nuclear translocation or binding of NF-κB to cognate motifs; rather, it functions in the nucleus by affecting the association of NF-κB with chromatin.
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U2 - 10.1074/jbc.M501928200
DO - 10.1074/jbc.M501928200
M3 - Article
C2 - 15799966
AN - SCOPUS:20444470299
SN - 0021-9258
VL - 280
SP - 22222
EP - 22232
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 23
ER -