The PYRIN domain in signal transduction

Christian Stehlik*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

17 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)293-310
Number of pages18
JournalCurrent Protein and Peptide Science
Volume8
Issue number3
DOIs
StatePublished - Jun 2007

Keywords

  • Apoptosis
  • CARD domain
  • Cancer
  • Caspase activation
  • Death domain fold
  • Inflammation
  • Interleukin-1
  • Leucine richregion
  • NACHT domain
  • NF-κB
  • PYRIN domain
  • Pathogen associated molecular pattern
  • Pathogen recognition receptor
  • Signaltransduction

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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