Phosphorylation of receptor-like cytoplasmic kinases by bacterial flagellin.
Molecular mechanisms that distinguish self and non-self are fundamental in innate immunity to prevent infections in plants and animals. Recognition of the conserved microbial components triggers immune responses against a broad spectrum of potential pathogens. In Arabidopsis, bacterial flagellin was perceived by a leucine-rich repeat-receptor-like kinase (LRR-RLK) FLS2. Upon flagellin perception, FLS2 forms a complex with another LRR-RLK BAK1. The intracellular signaling events downstream of FLS2/BAK1 receptor complex are still poorly understood. We recently identified a receptor-like cytoplasmic kinase (RLCK) BIK1 that associates with flagellin receptor complex to initiate plant innate immunity. BIK1 is rapidly phosphorylated upon flagellin perception in an FLS2- and BAK1-dependent manner. BAK1 directly phosphorylates BIK1 with an in vitro kinase assay. Plants have evolved a large number of RLCK genes involved in a wide range of biological processes. We provided evidence here that additional RLCKs could also be phosphorylated by flagellin and may play redundant role with BIK1 in plant innate immunity.
Lu
Dongping
D
Department of Plant Pathology and Microbiology (S.W. & L.S.), Department of Biochemistry and Biophysics (D.L & P.H.) and Institute for Plant Genomics and Biotechnology, Texas A&M University, College Station, TX USA.
Wu
Shujing
S
Department of Plant Pathology and Microbiology (S.W. & L.S.), Department of Biochemistry and Biophysics (D.L & P.H.) and Institute for Plant Genomics and Biotechnology, Texas A&M University, College Station, TX USA.
He
Ping
P
Department of Plant Pathology and Microbiology (S.W. & L.S.), Department of Biochemistry and Biophysics (D.L & P.H.) and Institute for Plant Genomics and Biotechnology, Texas A&M University, College Station, TX USA.
Shan
Libo
L
Department of Plant Pathology and Microbiology (S.W. & L.S.), Department of Biochemistry and Biophysics (D.L & P.H.) and Institute for Plant Genomics and Biotechnology, Texas A&M University, College Station, TX USA.
D001419:Bacteria / Q000378:metabolism*; D005408:Flagellin / Q000378:metabolism*; D008954:Models, Biological; D010766:Phosphorylation; D057865:Plant Immunity; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism*; D051192:Receptors, Pattern Recognition / Q000378:metabolism; D015398:Signal Transduction
D051192:Receptors, Pattern Recognition; D005408:Flagellin; D020794:Receptor Protein-Tyrosine Kinases
Nature. 2004 Feb 26;427(6977):858-61
14985766
Science. 2009 May 8;324(5928):742-4
19423812
Science. 2008 Jul 25;321(5888):557-60
18653891
Nat Immunol. 2006 Dec;7(12):1243-9
17110940
Cell Microbiol. 2007 Jun;9(6):1385-96
17451411
Cell. 2006 Feb 24;124(4):783-801
16497588
Science. 2003 Aug 29;301(5637):1230-3
12947197
Cell. 2006 Feb 24;124(4):803-14
16497589
Science. 2009 Nov 6;326(5954):850-3
19892983
Nature. 2007 Jul 26;448(7152):497-500
17625569
Proc Natl Acad Sci U S A. 2010 Jan 5;107(1):496-501
20018686
Plant Physiol. 2003 Jun;132(2):530-43
12805585
Genetics. 1999 May;152(1):401-12
10224270
Mol Cell. 2000 Jun;5(6):1003-11
10911994
Plant Cell. 2006 Jan;18(1):257-73
16339855
Plant Cell. 2006 Mar;18(3):764-79
16461584
Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):12217-22
17626179
Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10763-8
11526204
Nature. 2006 Nov 16;444(7117):323-9
17108957
Proc Natl Acad Sci U S A. 2009 Mar 24;106(12):4584-90
19264966