Defying death: showing Bcl-2 the way home

Bcl-2 and Bcl-x L perform important functions in cell life or death decisions by setting the threshold for activation of the programmed cell death machinery. FKBP38, a member of the immunophilin family, has now been identified as a new Bcl-2/Bcl-x L -binding partner. Furthermore, FKBP38 seems to be...

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Veröffentlicht in:	Nature cell biology 2003-01, Vol.5 (1), p.9-11
Hauptverfasser:	Adrain, Colin, Creagh, Emma M., Martin, Seamus J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Apoptosis Apoptosis - physiology bcl-X Protein Binding Sites Biomedical and Life Sciences Cancer Research Caspases - metabolism Cell Biology Developmental Biology Genetic aspects Genetic regulation Humans Immunophilins - metabolism Life Sciences Mitochondria - physiology Mitochondria - ultrastructure Mortality news-and-views Physiological aspects Proteases Proto-Oncogene Proteins c-bcl-2 - metabolism Proto-Oncogene Proteins c-bcl-2 - physiology Stem Cells Tacrolimus Binding Proteins - metabolism
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Beschreibung
Zusammenfassung:	Bcl-2 and Bcl-x L perform important functions in cell life or death decisions by setting the threshold for activation of the programmed cell death machinery. FKBP38, a member of the immunophilin family, has now been identified as a new Bcl-2/Bcl-x L -binding partner. Furthermore, FKBP38 seems to be crucial in targeting Bcl-2/Bcl-x L to the correct cellular locations.
ISSN:	1465-7392 1476-4679
DOI:	10.1038/ncb0103-9a