Universität zu Köln

Maekawa, Takaki, Kufer, Thomas A. and Schulze-Lefert, Paul (2011). NLR functions in plant and animal immune systems: so far and yet so close. Nat. Immunol., 12 (9). S. 818 - 827. NEW YORK: NATURE PUBLISHING GROUP. ISSN 1529-2916

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Abstract

In plants and animals, the NLR family of receptors perceives non-self and modified-self molecules inside host cells and mediates innate immune responses to microbial pathogens. Despite their similar biological functions and protein architecture, animal NLRs are normally activated by conserved microbe-or damage-associated molecular patterns, whereas plant NLRs typically detect strain-specific pathogen effectors. Plant NLRs recognize either the effector structure or effector-mediated modifications of host proteins. The latter indirect mechanism for the perception of non-self, as well as the within-species diversification of plant NLRs, maximize the capacity to recognize non-self through the use of a finite number of innate immunoreceptors. We discuss recent insights into NLR activation, signal initiation through the homotypic association of N-terminal domains and subcellular receptor dynamics in plants and compare those with NLR functions in animals.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Maekawa, Takaki UNSPECIFIED UNSPECIFIED UNSPECIFIED Kufer, Thomas A. UNSPECIFIED UNSPECIFIED UNSPECIFIED Schulze-Lefert, Paul UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-490002
DOI:	10.1038/ni.2083
Journal or Publication Title:	Nat. Immunol.
Volume:	12
Number:	9
Page Range:	S. 818 - 827
Date:	2011
Publisher:	NATURE PUBLISHING GROUP
Place of Publication:	NEW YORK
ISSN:	1529-2916
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language ARABIDOPSIS RESISTANCE PROTEIN; RICH REPEAT PROTEIN; NB-LRR PROTEIN; DISEASE-RESISTANCE; CELL-DEATH; MILDEW RESISTANCE; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; TIR DOMAIN; HYPERSENSITIVE RESPONSE Multiple languages Immunology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/49000