A new eye on NLR proteins: focused on clarity or diffused by complexity?

被引：115

作者：

Bonardi, Vera ^{[1
]}

Cherkis, Karen ^{[1
,3
]}

Nishimura, Marc T. ^{[1
]}

Dangl, Jeffery L. ^{[1
,2
,3
,4
,5
]}

机构：

[1] Univ N Carolina, Dept Biol, Chapel Hill, NC 27599 USA

[2] Howard Hughes Med Inst, Chapel Hill, NC 27599 USA

[3] Univ N Carolina, Curriculum Genet & Mol Biol, Chapel Hill, NC 27599 USA

[4] Univ N Carolina, Dept Microbiol & Immunol, Chapel Hill, NC 27599 USA

[5] Univ N Carolina, Carolina Ctr Genome Sci, Chapel Hill, NC 27599 USA

来源：

CURRENT OPINION IN IMMUNOLOGY | 2012年 / 24卷 / 01期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

DISEASE RESISTANCE PROTEIN; NB-LRR PROTEIN; IMMUNE-RECEPTOR RESISTANCE; TOBACCO-MOSAIC-VIRUS; OF-FUNCTION MUTATION; RICH REPEAT PROTEIN; CELL-DEATH; ATP BINDING; CONSTITUTIVE ACTIVATION; PATHOGEN RECOGNITION;

D O I：

10.1016/j.coi.2011.12.006

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

The nucleotide-binding domain /eucine-rich repeat proteins (NLRs) represent the major class of intracellular innate immune receptors in plants and animals. Understanding their functions is a major challenge in immunology. This review highlights recent efforts toward elucidating NLR functions in human and plants. We compare unconventional aspects of NLR proteins across the two kingdoms. We review recent advances describing P-loop independent activation, nuclear-cytoplasmic trafficking, oligonnerization and multimerization requirements for signaling, and for expanded functions beyond pathogen recognition by several NLR proteins.

引用

页码：41 / 50

页数：10

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