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Assembling the building blocks: structure and function of inhibitor of apoptosis proteins

P D Mace1, S Shirley, C L Day

  • 1Biochemistry Department, University of Otago, Dunedin 9054, New Zealand.

Cell Death and Differentiation
|April 18, 2009
PubMed

Insights

Inhibitor of apoptosis (IAP) proteins regulate cell death by controlling caspases. This review details IAP structural features and how their domains cooperate to modulate apoptosis, crucial for understanding cell survival and death.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Apoptosis, or programmed cell death, is tightly regulated by a balance of proapoptotic and prosurvival molecules.
  • Inhibitor of apoptosis (IAP) proteins are key negative regulators of apoptosis, acting by inhibiting caspases or their activation pathways.

Purpose of the Study:

  • To review the structural features of IAP proteins.
  • To discuss the functional contribution of each domain within IAP proteins.
  • To highlight the importance of domain cooperation in IAP activity.

Main Methods:

  • Literature review of IAP protein structure and function.
  • Analysis of IAP protein-protein interaction domains.
  • Examination of ubiquitination mechanisms (autoubiquitylation and substrate ubiquitination).

Main Results:

  • IAP proteins function as ubiquitin E3 ligases.
  • IAPs possess distinct protein-protein interaction domains crucial for their function.
  • The balance between autoubiquitylation and substrate ubiquitination is critical for IAP activity.

Conclusions:

  • Understanding IAP structural domains is essential for comprehending their role in apoptosis control.
  • Further research is needed to elucidate how IAP domains function in concert.
  • Deciphering domain interplay is key to advancing knowledge of these complex regulators of cell death.

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