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Effects of the BH3-only protein human Noxa on mitochondrial dynamics.

Authors
Woo, HN; Seo, YW; Moon, AR; Jeong, SY; Choi, EK; Kim, TH
Citation
FEBS letters, 583(14):2349-2354, 2009
Journal Title
FEBS letters
ISSN
0014-57931873-3468
Abstract
Mitochondria form reticular networks comprised of filamentous tubules and continuously move and change shape. Bcl-2 family proteins actively participate in the regulation of mitochondria fragmentation. Here, we show that human Noxa, which belongs to the BH3-only pro-apoptotic Bcl-2 family, causes mitochondrial fragmentation. We found that while the Bcl-2 homology 3 (BH3) domain of Noxa is not associated with mitochondrial fragmentation, the mitochondrial targeting domain (MTD) of Noxa is the region responsible for inducing fragmentation. Two leucine residues in MTD play a key role in the process. Furthermore, the lack of Noxa causes a significant reduction of Velcade-induced mitochondrial fragmentation. Together, these results provide novel insight into the role of Noxa in mitochondrial dynamics and cell death.
MeSH terms
Amino Acid SequenceAnimalsBoronic Acids/metabolismCell Death/physiologyHela CellsHumansLeucine/metabolismMitochondria/metabolism*Mitochondria/ultrastructureMolecular Sequence DataProtease Inhibitors/metabolismProto-Oncogene Proteins c-bcl-2/geneticsProto-Oncogene Proteins c-bcl-2/metabolism*Pyrazines/metabolismSignal Transduction/physiologybcl-2-Associated X Protein/metabolism
DOI
10.1016/j.febslet.2009.06.029
PMID
19540835
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Medical Genetics
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