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Publication : Cloning and characterization of a novel RING-B-box-coiled-coil protein with apoptotic function.

First Author  Kimura F Year  2003
Journal  J Biol Chem Volume  278
Issue  27 Pages  25046-54
PubMed ID  12692137 Mgi Jnum  J:84377
Mgi Id  MGI:2667505 Doi  10.1074/jbc.M303438200
Citation  Kimura F, et al. (2003) Cloning and characterization of a novel RING-B-box-coiled-coil protein with apoptotic function. J Biol Chem 278(27):25046-54
abstractText  We have identified a novel RING-B-box-coiled-coil (RBCC) protein (MAIR for macrophage-derived apoptosis-inducing RBCC protein) that consists of an N-terminal RING finger, followed by a B-box zinc finger, a coiled-coil domain, and a B30.2 domain. MAIR mRNA was expressed widely in mouse tissues and was induced by macrophage colony-stimulating factor in murine peritoneal and bone marrow macrophages. MAIR protein initially showed a granular distribution predominantly in the cytoplasm. The addition of zinc to transfectants containing MAIR cDNA as part of a heavy metal-inducible vector caused apoptosis of the cells characterized by cell fragmentation; a reduction in mitochondrial membrane potential; activation of caspase-7, -8, and -9, but not caspase-3; and DNA degradation. We also found that the RING finger and coiled-coil domains were required for MAIR activity by analysis with deletion mutants.
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