Research Update
PAAD – a new protein domain associated with apoptosis, cancer and autoimmune diseases

https://doi.org/10.1016/S0968-0004(00)01729-1Get rights and content

Abstract

A new protein domain was found in several proteins involved in apoptosis, inflammation, cancer and immune responses. Its location within these proteins and predicted fold suggests that it functions as a protein–protein interaction domain, possibly uniting different signaling pathways.

Section snippets

Acknowledgements

We thank Dr Weizhong Li for the continuous development of the Saturated BLAST program. K.P. and A.G. were supported by NIH grant GM60049.

References (20)

There are more references available in the full text version of this article.

Cited by (121)

  • COPs and POPs Patrol Inflammasome Activation

    2018, Journal of Molecular Biology
  • Identification of multifaceted binding modes for pyrin and ASC pyrin domains gives insights into pyrin inflammasome assembly

    2014, Journal of Biological Chemistry
    Citation Excerpt :

    The adaptor protein ASC plays a central role in assembly of the pyrin inflammasome, as well as the inflammasomes formed by several NLR and PYHIN family proteins (10). ASC consists of an N-terminal PYD and a C-terminal CARD, which is also a death fold domain (21, 26). A homotypic interaction between ASC PYD and the N-terminal PYDs of pyrin, NLRP1, NLRP3, NLRP7, and AIM2 recruits ASC to inflammasomes, whereas ASC CARD recruits procaspase-1 via a homotypic CARD interaction (10).

  • The PYHIN Family of Molecules and their Functions Sensing dsDNA

    2013, Biological DNA Sensor: The Impact of Nucleic Acids on Diseases and Vaccinology
  • NLRC5: A newly discovered MHC class I transactivator (CITA)

    2012, Microbes and Infection
    Citation Excerpt :

    At the C-terminus they contain leucine-rich repeats (LRRs), generally believed to act as sensors of danger signals or ligands of microbial origin. At the N-terminus they display a variable effector domain, which can consist of either a caspase recruitment domain (CARD), a pyrin domain (also known as PAAD, PYD or DAPIN) [20–26], an acidic domain, or a baculovirus inhibitor repeat (BIR) domain [17,27]. The major function of the NLR proteins is to initiate innate immune responses upon recognition of components of infecting pathogens [28].

View all citing articles on Scopus
View full text