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The Apaf-1 apoptosome: a large caspase-activating complex.

Kelvin Cain¹, Shawn B Bratton, Gerald M Cohen

¹MRC Toxicology Unit, Hodgkin Building, University of Leicester, PO Box 138, Lancaster Road, Leicester LE1 9HN, UK. kc5@le.ac.uk

|May 23, 2002

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The apoptosome, a large protein complex, is crucial for initiating apoptosis by activating caspases. Its assembly and function are tightly regulated by various cellular factors, ensuring it only forms when cell death is certain.

Area of Science:

Cellular Biology
Molecular Biology
Biochemistry

Background:

Key biological processes like apoptosis involve large multi-protein complexes.
Apoptosis initiation involves death receptors or mitochondria, leading to caspase activation.
Caspases, essential for apoptosis, require proteolytic processing within complexes like the apoptosome.

Purpose of the Study:

To elucidate the structure and function of the apoptosome in apoptosis.
To understand the role of Apaf-1 in apoptosome formation.
To investigate the regulation of apoptosome assembly and activity.

Main Methods:

Described apoptosome formation in apoptotic cells, cell lysates, and with recombinant proteins.
Identified Apaf-1 as the central scaffold protein.

Related Experiment Videos

Investigated regulation by K(+) levels, IAPs, heat shock proteins, and Smac/Diablo.

Main Results:

Apaf-1 oligomerizes with cytochrome c and dATP to form the apoptosome (700-1400 kDa).
The apoptosome recruits and processes caspase-9, activating effector caspases.
Apoptosome assembly and function are regulated by multiple factors, ensuring timely apoptosis.

Conclusions:

The apoptosome is a critical large protein complex in the caspase-dependent apoptosis pathway.
Regulation of apoptosome formation ensures its activity is restricted to cells committed to die.
Understanding apoptosome regulation provides insights into controlling cell death processes.