scholarly journals Nucleotide binding domain and leucine-rich repeat pyrin domain-containing protein 12: characterization of its binding to hematopoietic cell kinase

2020 ◽  
Vol 16 (9) ◽  
pp. 1507-1525 ◽  
Author(s):  
Yue Zhang ◽  
Curtis T. Okamoto
Keyword(s):  
Nucleotide Binding ◽  
Binding Domain ◽  
Hematopoietic Cell ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Pyrin Domain ◽  
Hematopoietic Cell Kinase

scholarly journals Broad detection of bacterial type III secretion system and flagellin proteins by the human NAIP/NLRC4 inflammasome

2017 ◽  
Vol 114 (50) ◽  
pp. 13242-13247 ◽  
Author(s):  
Valeria M. Reyes Ruiz ◽  
Jasmine Ramirez ◽  
Nawar Naseer ◽  
Nicole M. Palacio ◽  
Ingharan J. Siddarthan ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Bacterial Species ◽  
Type Iii Secretion System ◽  
Nucleotide Binding ◽  
Secretion System ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Type Iii ◽  
Needle Protein

Inflammasomes are cytosolic multiprotein complexes that initiate host defense against bacterial pathogens by activating caspase-1–dependent cytokine secretion and cell death. In mice, specific nucleotide-binding domain, leucine-rich repeat-containing family, apoptosis inhibitory proteins (NAIPs) activate the nucleotide-binding domain, leucine-rich repeat-containing family, CARD domain-containing protein 4 (NLRC4) inflammasome upon sensing components of the type III secretion system (T3SS) and flagellar apparatus. NAIP1 recognizes the T3SS needle protein, NAIP2 recognizes the T3SS inner rod protein, and NAIP5 and NAIP6 recognize flagellin. In contrast, humans encode a single functional NAIP, raising the question of whether human NAIP senses one or multiple bacterial ligands. Previous studies found that human NAIP detects both flagellin and the T3SS needle protein and suggested that the ability to detect both ligands was achieved by multiple isoforms encoded by the single humanNAIPgene. Here, we show that human NAIP also senses theSalmonellaTyphimurium T3SS inner rod protein PrgJ and that T3SS inner rod proteins from multiple bacterial species are also detected. Furthermore, we show that a single human NAIP isoform is capable of sensing the T3SS inner rod, needle, and flagellin. Our findings indicate that, in contrast to murine NAIPs, promiscuous recognition of multiple bacterial ligands is conferred by a single human NAIP.

scholarly journals Structural and Biochemical Characterization of a Cyclic Nucleotide Binding Domain from the EAG Family

2012 ◽  
Vol 102 (3) ◽  
pp. 330a
Author(s):  
Maria J. Marques Carvalho ◽  
Ricardo S. Vieira Pires ◽  
Guillaume Gabant ◽  
Martine Cadene ◽  
João H. Morais Cabral
Keyword(s):  
Cyclic Nucleotide ◽  
Biochemical Characterization ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Cyclic Nucleotide Binding ◽  
Cyclic Nucleotide Binding Domain
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