IAPs: Modular regulators of cell signalling

Rhesa Budhidarmo; Catherine L Day

doi:10.1016/j.semcdb.2014.12.002

IAPs: Modular regulators of cell signalling

Semin Cell Dev Biol. 2015 Mar:39:80-90. doi: 10.1016/j.semcdb.2014.12.002. Epub 2014 Dec 24.

Authors

Rhesa Budhidarmo¹, Catherine L Day²

Affiliations

¹ Department of Biochemistry, Otago School of Medical Sciences, University of Otago, Dunedin 9054, New Zealand.
² Department of Biochemistry, Otago School of Medical Sciences, University of Otago, Dunedin 9054, New Zealand. Electronic address: catherine.day@otago.ac.nz.

PMID: 25542341
DOI: 10.1016/j.semcdb.2014.12.002

Abstract

Members of the inhibitor of apoptosis (IAP) family are characterised by the presence of at least one baculoviral IAP repeat (BIR) domain. However, during the course of evolution, other globular modules have been adopted to perform distinct functions. Consequently, the IAP family is now recognised as consisting of members that perform critical functions in different aspects of cellular regulation. In this review, the structural diversity present within the IAP protein family is presented. Known structures of individual domains are discussed and their properties are described in light of recent data. In particular the plasticity of BIR domains and their ability to accommodate different binding partners is highlighted, as well as the importance of communication between the domains in regulating the covalent attachment of ubiquitin.

Keywords: BIR; Domain; IAP; RING; Ubiquitin.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Amino Acid Sequence
Animals
Cell Physiological Phenomena*
Humans
Inhibitor of Apoptosis Proteins / chemistry*
Inhibitor of Apoptosis Proteins / metabolism*
Models, Molecular
Molecular Sequence Data
Protein Interaction Domains and Motifs
Protein Structure, Tertiary
Sequence Alignment
Signal Transduction*

Substances

Inhibitor of Apoptosis Proteins