IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms.

doi:10.1038/ncb1204

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Article

IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms.

Nature cell biology - 1 Jan 2005

Tenev Tencho, Zachariou Anna, Wilson Rebecca, Ditzel Mark, Meier Pascal

Abstract excerpt

Some members of the inhibitor of apoptosis (IAP) family suppress apoptosis by neutralizing caspases. The current model suggests that all caspase-regulatory IAPs function as direct enzyme inhibitors, blocking effector caspases by binding to their catalytically active pockets. Here we show that IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms. Whereas XIAP binds...

Topics

Amino Acid Motifs
Animals
Apoptosis
Binding Sites
Caspase 7
Caspases
Drosophila Proteins
Drosophila melanogaster
Humans
Inhibitor of Apoptosis Proteins
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

NIH 3T3 Cells

Protein Binding

Protein Subunits

Proteins

Signal Transduction

Ubiquitin-Protein Ligases

Source

Open in PubMed

Identifiers

PMID: 15580265
DOI: 10.1038/ncb1204

Genes

XIAP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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