ARC1 Is an E3 Ubiquitin Ligase and Promotes the Ubiquitination of Proteins during the Rejection of Self-Incompatible <i>Brassica</i> Pollen

Stone, Sophia L.; Anderson, Erin M.; Mullen, Robert T.; Goring, Daphne R.

doi:10.1105/tpc.009845

Cited by 323 publications

(309 citation statements)

References 63 publications

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“…As discussed earlier, the U-box-containing proteins are newly identified E3 ubiquitin ligases that are present in yeast, plants, animals, and humans [35,62,63]. However, the number of U-box proteins varies among different organisms with a larger number of such proteins existing in the plant genomes.…”

Section: U-box-type E3 Ligases Are Newly Identified Members Of the Ubmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.

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Section: U-box-type E3 Ligases Are Newly Identified Members Of the Ubmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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“…We have previously shown that transient coexpression of Brassica SRK 910 with Brassica ARC1 in tobacco BY-2 cells resulted in relocalization of Brassica ARC1 from the cytosol/nucleus to endoplasmic reticulum (ER)-associated proteasomes (Stone et al, 2003;Fig. 3, M and S).…”

Section: The Effect Of Active Kinases On the Subcellular Localizationmentioning

confidence: 99%

Interactions between theS-Domain Receptor Kinases and AtPUB-ARM E3 Ubiquitin Ligases Suggest a Conserved Signaling Pathway in Arabidopsis

et al. 2008

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The Arabidopsis (Arabidopsis thaliana) genome encompasses multiple receptor kinase families with highly variable extracellular domains. Despite their large numbers, the various ligands and the downstream interacting partners for these kinases have been deciphered only for a few members. One such member, the S-receptor kinase, is known to mediate the self-incompatibility (SI) response in Brassica. S-receptor kinase has been shown to interact and phosphorylate a U-box/ARM-repeat-containing E3 ligase, ARC1, which, in turn, acts as a positive regulator of the SI response. In an effort to identify conserved signaling pathways in Arabidopsis, we performed yeast two-hybrid analyses of various S-domain receptor kinase family members with representative Arabidopsis plant U-box/ARM-repeat (AtPUB-ARM) E3 ligases. The kinase domains from S-domain receptor kinases were found to interact with ARM-repeat domains from AtPUB-ARM proteins. These kinase domains, along with M-locus protein kinase, a positive regulator of SI response, were also able to phosphorylate the ARM-repeat domains in in vitro phosphorylation assays. Subcellular localization patterns were investigated using transient expression assays in tobacco (Nicotiana tabacum) BY-2 cells and changes were detected in the presence of interacting kinases. Finally, potential links to the involvement of these interacting modules to the hormone abscisic acid (ABA) were investigated. Interestingly, AtPUB9 displayed redistribution to the plasma membrane of BY-2 cells when either treated with ABA or coexpressed with the active kinase domain of ARK1. As well, T-DNA insertion mutants for ARK1 and AtPUB9 lines were altered in their ABA sensitivity during germination and acted at or upstream of ABI3, indicating potential involvement of these proteins in ABA responses.

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“…The end result of this pathway is pollen rejection by preventing compatible pollen responses such as pollen grain hydration and pollen tube penetration into the stigma (described under compatible pollinations; Dickinson 1995 ). Following SCR/SP11 binding to SRK, the SRK-MLPK complex is proposed to recruit the ARM repeat-containing 1 (ARC1 ) E3-ubiquitin ligase (Stone et al 2003 ;Samuel et al 2008 ). B. napus ARC1 was the fi rst downstream signaling component identifi ed for SRK and was shown to be required for the rejection of self-pollen (Gu et al 1998 ;Stone et al 1999 ).…”

Section: Self-incompatibility In the Genus Arabidopsismentioning

confidence: 99%

“…Following from this, the role of ARC1 in the self-incompatibility pathway was proposed to promote the ubiquitination and degradation of the proposed compatibility factors by the 26S proteasome (Stone et al 2003 ). Through an ARC1-interaction screen, Exo70A1 was identifi ed as a candidate compatibility factor targeted by ARC1 (Samuel et al 2009 ).…”

Section: Self-incompatibility In the Genus Arabidopsismentioning

confidence: 99%

Signaling Events in Pollen Acceptance or Rejection in the Arabidopsis Species

Indriolo

Safavian

Goring

2014

Sexual Reproduction in Animals and Plants

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The initial events of pollen-pistil interactions are fundamentally important in fl owering plants because they infl uence successful fertilization. These early events include the recognition of pollen grains through signaling events in the pistil that will lead to the acceptance of a compatible pollen grain or the rejection of an incompatible pollen grain. There has been much research into this fi eld in the Brassicaceae, as this family includes many agriculturally important crops such as canola, radish, turnip, and cabbage. However, this review focuses on what is known about the early pollen-pistil interactions in the experimentally tractable Arabidopsis genus, including Arabidopsis thaliana (a self-compatible species) and Arabidopsis lyrata (a self-incompatible species). Compatible pollinations are driven by the ability of the pistil to provide the resources for an acceptable pollen grain to hydrate, germinate, and fertilize the ovule. Self-incompatible species have a receptorligand signaling pathway that rejects self-pollen grains, preventing inbreeding and encouraging genetic diversity within the species. There is some overlap between these two pathways, and current research is looking for unknown elements and downstream events following the initial recognition of a pollen grain in Arabidopsis .

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ARC1 Is an E3 Ubiquitin Ligase and Promotes the Ubiquitination of Proteins during the Rejection of Self-Incompatible Brassica Pollen

Cited by 323 publications

References 63 publications

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

Interactions between theS-Domain Receptor Kinases and AtPUB-ARM E3 Ubiquitin Ligases Suggest a Conserved Signaling Pathway in Arabidopsis

Signaling Events in Pollen Acceptance or Rejection in the Arabidopsis Species

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