2005
DOI: 10.1038/sj.emboj.7600910
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Adi3 is a Pdk1-interacting AGC kinase that negatively regulates plant cell death

Abstract: Bacterial speck disease in tomato is caused by Pseudomonas syringae pv. tomato. Resistance to this disease is conferred by the host Pto kinase, which recognizes P. s. pv. tomato strains that express the effector AvrPto. We report here that an AvrPto‐dependent Pto‐interacting protein 3 (Adi3) is a member of the AGC family of protein kinases. In mammals, AGC kinases are regulated by 3‐phosphoinositide‐dependent protein kinase‐1 (Pdk1). We characterized tomato Pdk1 and showed that Pdk1 and Pto phosphorylate Adi3.… Show more

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Cited by 76 publications
(148 citation statements)
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“…Direct regulators and executors of PCD in plants have also been identified by their PCD suppressing activity when they are overexpressed in animals, yeasts, and plants. These include an endoplasmic reticulumassociated BAX INHIBITOR-1 (BI-1; Kawai-Yamada et al, 2001;Watanabe and Lam, 2006;Ihara-Ohori et al, 2007), a transcription factor AtEBP (Pan et al, 2001;Ogawa et al, 2005), a vesicle-associated protein VAMP (Levine et al, 2001), and an AGC kinase Adi3 (Devarenne et al, 2006). These proteins possess a diverse variety of biochemical activities and localize to different cellular compartments, suggesting the involvement of many biochemical and cellular processes in regulating or executing PCD.…”
Section: Regulation Of Cell Death and Defense By The Bap And Bon Protmentioning
confidence: 99%
“…Direct regulators and executors of PCD in plants have also been identified by their PCD suppressing activity when they are overexpressed in animals, yeasts, and plants. These include an endoplasmic reticulumassociated BAX INHIBITOR-1 (BI-1; Kawai-Yamada et al, 2001;Watanabe and Lam, 2006;Ihara-Ohori et al, 2007), a transcription factor AtEBP (Pan et al, 2001;Ogawa et al, 2005), a vesicle-associated protein VAMP (Levine et al, 2001), and an AGC kinase Adi3 (Devarenne et al, 2006). These proteins possess a diverse variety of biochemical activities and localize to different cellular compartments, suggesting the involvement of many biochemical and cellular processes in regulating or executing PCD.…”
Section: Regulation Of Cell Death and Defense By The Bap And Bon Protmentioning
confidence: 99%
“…Moreover, PID, which is an auto-activating kinase (autophosporylation), may not need PDK1 during normal development (Sauer et al, 2006). Although PDK1 increases both trans-phosphorylation and autophosphorylation of several AGCVIII kinases in vitro (Anthony et al, 2006;Devarenne et al, 2006), its role in polar PIN localization remains to be deciphered.…”
Section: Signaling To Agc1 Kinasesmentioning
confidence: 99%
“…As might be expected because of its role as a key regulator of AGC kinase signaling, loss of PDK1 is lethal in yeast Niederberger and Schweingruber, 1999), Drosophila melanogaster (Rintelen et al, 2001), mouse (Lawlor et al, 2002), and tomato (Solanum lycopersicum; Devarenne et al, 2006). Interestingly, in contrast to the other studied PDK1 genes, Arabidopsis PDK1 (AtPDK1) appears to be nonessential for plant survival (Camehl et al, 2011).…”
mentioning
confidence: 99%
“…The second phosphorylation site is a Ser or Thr located in a region of variable length referred to as the activation loop or T-loop (Bö gre et al, 2003). In many AGC kinases from both mammals (Bayascas, 2008(Bayascas, , 2010 and plants (Bö gre et al, 2003;Anthony et al, 2004Anthony et al, , 2006Devarenne et al, 2006;Zegzouti et al, 2006aZegzouti et al, , 2006b), this activation loop site is phosphorylated by 3-phosphoinositide-dependent protein kinase 1 (PDK1). Activation loop phosphorylation by PDK1 typically occurs after docking of the phosphorylated hydrophobic motif of the AGC kinase substrate within a pocket located in the small lobe of the PDK1 kinase domain .…”
mentioning
confidence: 99%