Adi3 is a Pdk1-interacting AGC kinase that negatively regulates plant cell death

Devarenne, Timothy P.; Ekengren, Sophia; Pedley, Kerry F.; Martin, Gregory B.

doi:10.1038/sj.emboj.7600910

Cited by 76 publications

(148 citation statements)

References 50 publications

(97 reference statements)

Supporting

Mentioning

142

Contrasting

Order By: Relevance

“…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%

The ArabidopsisBAP1andBAP2Genes Are General Inhibitors of Programmed Cell Death

Yang

et al. 2007

Plant Physiology

View full text Add to dashboard Cite

Here we identify the BAP1 and BAP2 genes of Arabidopsis (Arabidopsis thaliana) as general inhibitors of programmed cell death (PCD) across the kingdoms. These two homologous genes encode small proteins containing a calcium-dependent phospholipid-binding C2 domain. BAP1 and its functional partner BON1 have been shown to negatively regulate defense responses and a disease resistance gene SNC1. Genetic studies here reveal an overlapping function of the BAP1 and BAP2 genes in cell death control. The loss of BAP2 function induces accelerated hypersensitive responses but does not compromise plant growth or confer enhanced resistance to virulent bacterial or oomycete pathogens. The loss of both BAP1 and BAP2 confers seedling lethality mediated by PAD4 and EDS1, two regulators of cell death and defense responses. Overexpression of BAP1 or BAP2 with their partner BON1 inhibits PCD induced by pathogens, the proapototic gene BAX, and superoxide-generating paraquat in Arabidopsis or Nicotiana benthamiana. Moreover, expressing BAP1 or BAP2 in yeast (Saccharomyces cerevisiae) alleviates cell death induced by hydrogen peroxide. Thus, the BAP genes function as general negative regulators of PCD induced by biotic and abiotic stimuli including reactive oxygen species. The dual roles of BAP and BON genes in repressing defense responses mediated by disease resistance genes and in inhibiting general PCD has implications in understanding the evolution of plant innate immunity.

show abstract

Section: Regulation Of Cell Death and Defense By The Bap And Bon Protmentioning

confidence: 99%

The ArabidopsisBAP1andBAP2Genes Are General Inhibitors of Programmed Cell Death

Yang

et al. 2007

Plant Physiology

View full text Add to dashboard Cite

show abstract

“…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%

Regulation of the Polarity of Protein Trafficking by Phosphorylation

Ganguly

Sasayama

Cho

2012

Molecules and Cells

View full text Add to dashboard Cite

The asymmetry of environmental stimuli and the execution of developmental programs at the organism level require a corresponding polarity at the cellular level, in both unicellular and multicellular organisms. In plants, cell polarity is important in major developmental processes such as cell division, cell enlargement, cell morphogenesis, embryogenesis, axis formation, organ development, and defense. One of the most important factors controlling cell polarity is the asymmetric distribution of polarity determinants. In particular, phosphorylation is implicated in the polar distribution of the determinant protein factors, a mechanism conserved in both prokaryotes and eukaryotes. In plants, formation of local gradients of auxin, the morphogenic hormone, is critical for plant developmental processes exhibiting polarity. The auxin efflux carriers PIN-FORMEDs (PINs) localize asymmetrically in the plasma membrane and cause the formation of local auxin gradients throughout the plant. The asymmetry of PIN distribution in the plasma membrane is determined by phosphorylationmediated polar trafficking of PIN proteins. This review discusses recent studies on the role of phosphorylation in polar PIN trafficking.

show abstract

“…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%

Characterization of a PDK1 Homologue from the Moss Physcomitrella patens

Dittrich

Devarenne

2011

Plant Physiology

View full text Add to dashboard Cite

The serine/threonine protein kinase 3-phosphoinositide-dependent protein kinase 1 (PDK1) is a highly conserved eukaryotic kinase that is a central regulator of many AGC kinase subfamily members. Through its regulation of AGC kinases, PDK1 controls many basic cellular processes, from translation to cell survival. While many of these PDK1-regulated processes are conserved across kingdoms, it is not well understood how PDK1 may have evolved within kingdoms. In order to better understand PDK1 evolution within plants, we have isolated and characterized the PDK1 gene from the moss Physcomitrella patens (PpPDK1), a nonvascular representative of early land plants. PpPDK1 is similar to other plant PDK1s in that it can functionally complement a yeast PDK1 knockout line. However, unlike PDK1 from other plants, the P. patens PDK1 protein does not bind phospholipids due to a lack of the lipid-binding pleckstrin homology domain, which is used for lipid-mediated regulation of PDK1 activity. Sequence analysis of several PDK1 proteins suggests that lipid regulation of PDK1 may not commonly occur in algae and nonvascular land plants. PpPDK1 can phosphorylate AGC kinase substrates from tomato (Solanum lycopersicum) and P. patens at the predicted PDK1 phosphorylation site, indicating that the PpPDK1 substrate phosphorylation site is conserved with higher plants. We have also identified residues within the PpPDK1 kinase domain that affect kinase activity and show that a mutant with highly reduced kinase activity can still confer cell viability in both yeast and P. patens. These studies lay the foundation for further analysis of the evolution of PDK1 within plants.

show abstract

Adi3 is a Pdk1-interacting AGC kinase that negatively regulates plant cell death

Cited by 76 publications

References 50 publications

The ArabidopsisBAP1andBAP2Genes Are General Inhibitors of Programmed Cell Death

The ArabidopsisBAP1andBAP2Genes Are General Inhibitors of Programmed Cell Death

Regulation of the Polarity of Protein Trafficking by Phosphorylation

Characterization of a PDK1 Homologue from the Moss Physcomitrella patens

Contact Info

Product

Resources

About