NB-LRR proteins: Pairs, pieces, perception, partners and pathways
Identifieur interne : 000376 ( Pmc/Corpus ); précédent : 000375; suivant : 000377NB-LRR proteins: Pairs, pieces, perception, partners and pathways
Auteurs : Timothy K. Eitas ; Jeffery L. DanglSource :
- Current opinion in plant biology [ 1369-5266 ] ; 2010.
Abstract
In plants, many of the innate immune receptors or disease resistance (R) proteins contain a NB-LRR (Nucleotide-binding site, Leucine-rich repeat) structure. The recent findings regarding NB-LRR signaling are summarized in this article. An emerging theme is that two NB-LRRs can function together to mediate disease resistance against pathogen isolates. Also, recent results delineate which NB-LRR protein fragments are sufficient to initiate defense signaling. Importantly, distinct fragments of different NB-LRRs are sufficient for function. Finally, we describe the new roles of accessory proteins and downstream host genes in NB-LRR signaling.
Url:
DOI: 10.1016/j.pbi.2010.04.007
PubMed: 20483655
PubMed Central: 2910844
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<front><journal-meta><journal-id journal-id-type="nlm-journal-id">100883395</journal-id><journal-id journal-id-type="pubmed-jr-id">21113</journal-id><journal-id journal-id-type="nlm-ta">Curr Opin Plant Biol</journal-id><journal-title>Current opinion in plant biology</journal-title><issn pub-type="ppub">1369-5266</issn><issn pub-type="epub">1879-0356</issn></journal-meta><article-meta><article-id pub-id-type="pmid">20483655</article-id><article-id pub-id-type="pmc">2910844</article-id><article-id pub-id-type="doi">10.1016/j.pbi.2010.04.007</article-id><article-id pub-id-type="manuscript">NIHMS199453</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>NB-LRR proteins: Pairs, pieces, perception, partners and pathways</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Eitas</surname><given-names>Timothy K.</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Dangl</surname><given-names>Jeffery L.</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref><xref ref-type="aff" rid="A3">3</xref><xref ref-type="aff" rid="A4">4</xref></contrib></contrib-group><aff id="A1"><label>1</label>Curriculum in Genetics and Molecular Biology, University of North Carolina, Chapel Hill, NC 27599, USA</aff><aff id="A2"><label>2</label>Department of Biology, University of North Carolina, Chapel Hill, NC 27599, USA</aff><aff id="A3"><label>3</label>Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27599, USA</aff><aff id="A4"><label>4</label>Carolina Center for Genome Sciences, University of North Carolina, Chapel Hill, NC 27599, USA</aff><author-notes><corresp id="CR1">Correspondence author: Jeff Dangl, Department of Biology, 108 Coker Hall, University of North Carolina, CB#3280, Chapel Hill, NC 27599-3280, USA. <email>dangl@email.unc.edu</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>3</day><month>5</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>17</day><month>5</month><year>2010</year></pub-date><pub-date pub-type="ppub"><day>1</day><month>8</month><year>2010</year></pub-date><pub-date pub-type="pmc-release"><day>1</day><month>8</month><year>2011</year></pub-date><volume>13</volume><issue>4</issue><fpage>472</fpage><lpage>477</lpage><permissions><copyright-statement>© 2010 Elsevier Ltd. All rights reserved.</copyright-statement><copyright-year>2010</copyright-year></permissions><abstract><title>SUMMARY OF RECENT ADVANCES</title><p id="P1">In plants, many of the innate immune receptors or disease resistance (R) proteins contain a NB-LRR (Nucleotide-binding site, Leucine-rich repeat) structure. The recent findings regarding NB-LRR signaling are summarized in this article. An emerging theme is that two NB-LRRs can function together to mediate disease resistance against pathogen isolates. Also, recent results delineate which NB-LRR protein fragments are sufficient to initiate defense signaling. Importantly, distinct fragments of different NB-LRRs are sufficient for function. Finally, we describe the new roles of accessory proteins and downstream host genes in NB-LRR signaling.</p></abstract><contract-num rid="GM1">R01 GM066025-07
||GM</contract-num><contract-num rid="GM1">R01 GM057171-11
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