Abstract
The Death Domain Fold superfamily of evolutionarily conserved protein-protein interaction domains consists of 4 subfamilies: the death domain, the death effector domain, the caspase recruitment domain, and the PYRIN domain. Interaction of Death Domain Fold containing proteins modulates the activity of several downstream effectors, such as caspases and transcription factors. Recent studies provide evidence for not only homotypic-, but also heterotypic interactions among different sub-families, and even unconventional non-death domain fold interactions. As the number of potential protein associations among Death Domain Fold containing proteins expands and their influence on cellular responses increases, a challenging field for new investigations opens up. This review will focus on PYRIN domain-containing proteins and discuss the recent advances that provide strong evidence that PYRIN domain-mediated signal transduction has broad implications on cellular functions, including innate immunity, inflammation, differentiation, apoptosis, and cancer.
Keywords: Apoptosis, cancer, CARD domain, caspase activation, death domain fold, inflammation, interleukin-1, leucine rich region, NACHT domain, NF-κB
Current Protein & Peptide Science
Title: The PYRIN Domain in Signal Transduction
Volume: 8 Issue: 3
Author(s): Christian Stehlik
Affiliation:
Keywords: Apoptosis, cancer, CARD domain, caspase activation, death domain fold, inflammation, interleukin-1, leucine rich region, NACHT domain, NF-κB
Abstract: The Death Domain Fold superfamily of evolutionarily conserved protein-protein interaction domains consists of 4 subfamilies: the death domain, the death effector domain, the caspase recruitment domain, and the PYRIN domain. Interaction of Death Domain Fold containing proteins modulates the activity of several downstream effectors, such as caspases and transcription factors. Recent studies provide evidence for not only homotypic-, but also heterotypic interactions among different sub-families, and even unconventional non-death domain fold interactions. As the number of potential protein associations among Death Domain Fold containing proteins expands and their influence on cellular responses increases, a challenging field for new investigations opens up. This review will focus on PYRIN domain-containing proteins and discuss the recent advances that provide strong evidence that PYRIN domain-mediated signal transduction has broad implications on cellular functions, including innate immunity, inflammation, differentiation, apoptosis, and cancer.
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Cite this article as:
Stehlik Christian, The PYRIN Domain in Signal Transduction, Current Protein & Peptide Science 2007; 8 (3) . https://dx.doi.org/10.2174/138920307780831857
DOI https://dx.doi.org/10.2174/138920307780831857 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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