Correction: Protein Poly(ADP-ribosyl)ation Regulates Arabidopsis Immune Gene Expression and Defense Responses

Feng, Baomin; Liu, Chenglong; Oliveira, Marcos V. V. de; Intorne, Aline Chaves; Li, Bo; Babilonia, Kevin; Filho, Gonçalo Apolinário de Souza; Shan, Libo; He, Ping

doi:10.1371/journal.pgen.1005294

Cited by 2 publications

(2 citation statements)

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“…Protein ADP-ribosylation remains a poorly characterized PTM in plants. Although enzymes of the ADP-ribosyl transferase family are conserved in all land plants ( Lamb et al, 2012 ; Vainonen et al, 2016 ), only few ADP-ribosylated acceptor proteins have been characterized ( Feng et al, 2015 , 2016 ). In addition, the consequences of protein ADP-ribosylation in plants remain largely unknown.…”

Section: Introductionmentioning

confidence: 99%

“…The Arabidopsis thaliana genome encodes three PARP proteins (annotated as PARP1-3) with 27–47% sequence identity to Hs PARP-1 and Hs PARP-2. Arabidopsis PARP1 and PARP2 are active enzymes while direct evidence for PARP3 ADP-ribosyl transferase activity is lacking ( Babiychuk et al, 1998 ; Feng et al, 2015 ). Treatment of Arabidopsis with γ-radiation or genotoxic agents activates PARP1 and PARP2 ( Song et al, 2015 ).…”

Section: Introductionmentioning

confidence: 99%

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Nuclear Import of Arabidopsis Poly(ADP-Ribose) Polymerase 2 Is Mediated by Importin-α and a Nuclear Localization Sequence Located Between the Predicted SAP Domains

et al. 2018

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Proteins of the Poly(ADP-Ribose) Polymerase (PARP) family modify target proteins by covalent attachment of ADP-ribose moieties onto amino acid side chains. In Arabidopsis, PARP proteins contribute to repair of DNA lesions and modulate plant responses to various abiotic and biotic stressors. Arabidopsis PARP1 and PARP2 are nuclear proteins and given that their molecular weights exceed the diffusion limit of nuclear pore complexes, an active import mechanism into the nucleus is likely. Here we use confocal microscopy of fluorescent protein-tagged Arabidopsis PARP2 and PARP2 deletion constructs in combination with site-directed mutagenesis to identify a nuclear localization sequence in PARP2 that is required for nuclear import. We report that in co-immunoprecipitation assays PARP2 interacts with several isoforms of the importin-α group of nuclear transport adapters and that PARP2 binding to IMPORTIN-α2 is mediated by the identified nuclear localization sequence. Our results demonstrate that PARP2 is a cargo protein of the canonical importin-α/β nuclear import pathway.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Nuclear Import of Arabidopsis Poly(ADP-Ribose) Polymerase 2 Is Mediated by Importin-α and a Nuclear Localization Sequence Located Between the Predicted SAP Domains

et al. 2018

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An Arabidopsis Lipid Flippase Is Required for Timely Recruitment of Defenses to the Host–Pathogen Interface at the Plant Cell Surface

2017

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Deposition of cell wall-reinforcing papillae is an integral component of the plant immune response. The Arabidopsis PENETRATION 3 (PEN3) ATP binding cassette (ABC) transporter plays a role in defense against numerous pathogens and is recruited to sites of pathogen detection where it accumulates within papillae. However, the trafficking pathways and regulatory mechanisms contributing to recruitment of PEN3 and other defenses to the host-pathogen interface are poorly understood. Here, we report a confocal microscopy-based screen to identify mutants with altered localization of PEN3-GFP after inoculation with powdery mildew fungi. We identified a mutant, aberrant localization of PEN3 3 (alp3), displaying accumulation of the normally plasma membrane (PM)-localized PEN3-GFP in endomembrane compartments. The mutant was found to be disrupted in the P-ATPase AMINOPHOSPHOLIPID ATPASE 3 (ALA3), a lipid flippase that plays a critical role in vesicle formation. We provide evidence that PEN3 undergoes continuous endocytic cycling from the PM to the trans-Golgi network (TGN). In alp3, PEN3 accumulates in the TGN, causing delays in recruitment to the host-pathogen interface. Our results indicate that PEN3 and other defense proteins continuously cycle through the TGN and that timely exit of these proteins from the TGN is critical for effective pre-invasive immune responses against powdery mildews.

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Correction: Protein Poly(ADP-ribosyl)ation Regulates Arabidopsis Immune Gene Expression and Defense Responses

Cited by 2 publications

References 1 publication

Nuclear Import of Arabidopsis Poly(ADP-Ribose) Polymerase 2 Is Mediated by Importin-α and a Nuclear Localization Sequence Located Between the Predicted SAP Domains

Nuclear Import of Arabidopsis Poly(ADP-Ribose) Polymerase 2 Is Mediated by Importin-α and a Nuclear Localization Sequence Located Between the Predicted SAP Domains

An Arabidopsis Lipid Flippase Is Required for Timely Recruitment of Defenses to the Host–Pathogen Interface at the Plant Cell Surface

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