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Applied Biochemistry and Biotechnology

, Volume 172, Issue 8, pp 3902–3912 | Cite as

Self-oligomerization of ASC PYD Domain Prevents the Assembly of Inflammasome In Vitro

  • Kannan Badri Narayanan
  • Tae-Ho Jang
  • Hyun Ho ParkEmail author
Article

Abstract

NALP3 inflammasome, which is an inflammatory caspase-activating complex, is composed of three proteins: NALP3 (an NOD-like receptor), an apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), and caspase-1. NALP3 senses danger signals, while ASC is an adaptor molecule containing two protein interaction modules: pyrin domain (PYD) and caspase recruitment domain (CARD). Caspase-1 is a cysteine protease that uses cysteine as a nucleophile and has a CARD domain for protein interaction. During inflammasome formation, the ASC adaptor acts as a bridge between caspase and NOD-like receptor (NLR) by offering the CARD for CARD–CARD interactions and PYD for PYD–PYD interactions. In the current study, we successfully purified and characterized NALP3 PYD and ASC PYD. The results showed that ASC PYD easily self-oligomerized under physiological conditions, and this self-oligomerization of the ASC PYD prevented complex formation with NALP3 PYD in vitro.

Keywords

Inflammation Inflammasome Caspase-1 NALP3 ASC 

Notes

Acknowledgments

This study was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) of the Ministry of Education, Science and Technology (2013009083) and a grant from the Korea Healthcare Technology R&D project, Ministry of Health & Welfare, Republic of Korea (HI13C1449).

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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  • Kannan Badri Narayanan
    • 1
  • Tae-Ho Jang
    • 1
  • Hyun Ho Park
    • 1
    Email author
  1. 1.Department of Biochemistry, School of Biotechnology and Graduate School of BiochemistryYeungnam UniversityGyeongsanSouth Korea

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