Control of mitochondrial integrity by XXXX family members and caspase-independent cell death.

@entity204 @entity462 @entity588
@entity204 ( @entity204 ) is essential for normal development and maintenance of tissue homeostasis in multicellular organisms. While it is now evident that @entity204 can take many different forms, apoptosis is probably the most well-defined cell death programme. The characteristic morphological and biochemical features associated with this highly regulated form of cell death have until recently been exclusively attributed to the caspase family of @entity462 proteases. As a result, many investigators affiliate apoptosis with its pivotal execution system, i.e. caspase activation. However, it is becoming increasingly clear that @entity204 or apoptosis can also proceed in a caspase-independent manner and maintain key characteristics of apoptosis. Mitochondrial integrity is central to both caspase-dependent and-independent cell death. The release of pro-apoptotic factors from the mitochondrial intermembrane space is a key event in a cell's commitment to die and is under the tight regulation of the @entity588 family. However, the underlying mechanisms governing the efflux of these pro-death molecules are largely unknown. This review will focus on the regulation of mitochondrial integrity by @entity588 family members with particular attention to the controlled release of factors involved in caspase-independent cell death.
