Multifunctional Arm Repeat Domains in Plants

Samuel, Marcus A.; Salt, Jennifer N.; Shiu, Shin-Han; Goring, Daphne R.

doi:10.1016/s0074-7696(06)53001-3

Cited by 67 publications

(70 citation statements)

References 110 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…One of these interactors, ARC1, is a U-box, ARM-repeatcontaining protein with E3 ligase activity, and was found to be a positive regulator of the SI response (Stone et al, 1999(Stone et al, , 2003. Analyses of the Arabidopsis genome for proteins with U-box and ARM domains revealed a gene family with 41 AtPUB-ARM members (Azevedo et al, 2001;Mudgil et al, 2004;Samuel et al, 2006). In this article, we have found that the AtPUB-ARM proteins are able to interact with SD1 receptor kinases, suggesting a conservation of interaction/signaling components across species.…”

Section: Discussionmentioning

confidence: 99%

“…AtPUB9, 29, and 38 were selected to represent AtPUB-ARM proteins that lack the UND domain (U-box and ARM only), and AtPUB9 and 38 are more closely related to ARC1 relative to AtPUB29. Finally, AtPUB44 was chosen to represent the dual ARM-repeat clade (U-box:ARM:ARM) and is the most distantly related AtPUB relative to ARC1 (Mudgil et al, 2004;Samuel et al, 2006). All six of these AtPUB-ARM proteins have been shown to have in vitro E3 ubiquitin ligase activity (Andersen et al, 2004;Mudgil et al, 2004;J.…”

Section: Atpub-arm Proteins Interact With Arabidopsis and Brassica S-mentioning

confidence: 99%

“…ARC1 and AtPUB13 have a similar domain organization with the UND: U-box:ARM domains, whereas AtPUB9 contains only the U-Box:ARM domains ( Fig. 1A; Samuel et al, 2006). The PUB-ARM proteins were expressed as GFP fusions and the cytosolic kinase domains were expressed as red fluorescent protein (RFP):ARK1, GST:ARK2, and MLPK:MYC fusion proteins.…”

Section: The Effect Of Active Kinases On the Subcellular Localizationmentioning

confidence: 99%

“…The plant U-box (PUB) family can be divided into five groups based on the presence of other distinguishing domains, such as the UFD2, ARM repeats, UND, Ser/Thr kinase, WD40 repeats (Azevedo et al, 2001;Mudgil et al, 2004;Wiborg et al, 2008). The PUB-ARM family comprises the largest group with 41 predicted members in the Arabidopsis genome and 43 members in the rice (Oryza sativa) genome (Mudgil et al, 2004;Samuel et al, 2006). Despite the limited knowledge about the biological functions for these predicted PUB-ARM proteins, they have been shown to function as E3 ubiquitin ligases (Andersen et al, 2004;Mudgil et al, 2004).…”

mentioning

confidence: 99%

See 3 more Smart Citations

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

et al. 2008

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Atpub-arm Proteins Interact With Arabidopsis and Brassica S-mentioning

confidence: 99%

Section: The Effect Of Active Kinases On the Subcellular Localizationmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

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

et al. 2008

Self Cite

View full text Add to dashboard Cite

show abstract

“…The U-box/ARM proteins interacting with these RLKs belong to the Plant U-Box (PUB) family of putative E3 ubiquitin ligases (Mudgil et al, 2004). The overall identity between these two proteins is 50% (66% similarity), but their ARM repeats, a well-known protein-protein interaction domain (Andrade et al, 2001;Samuel et al, 2006), are much more conserved, with 74% identity (83% similarity). A truncated version of Os08g01900 containing mainly the ARM domain was recovered from the library screening using the kinase domain of Os08g03020 as bait (Supplemental Table S2).…”

Section: Rlk/pelle Family Member-e3 Ubiquitin Ligase Interactions In mentioning

confidence: 99%

A Rice Kinase-Protein Interaction Map

et al. 2008

View full text Add to dashboard Cite

Plants uniquely contain large numbers of protein kinases, and for the vast majority of the 1,429 kinases predicted in the rice (Oryza sativa) genome, little is known of their functions. Genetic approaches often fail to produce observable phenotypes; thus, new strategies are needed to delineate kinase function. We previously developed a cost-effective high-throughput yeast twohybrid system. Using this system, we have generated a protein interaction map of 116 representative rice kinases and 254 of their interacting proteins. Overall, the resulting interaction map supports a large number of known or predicted kinaseprotein interactions from both plants and animals and reveals many new functional insights. Notably, we found a potential widespread role for E3 ubiquitin ligases in pathogen defense signaling mediated by receptor-like kinases, particularly by the kinases that may have evolved from recently expanded kinase subfamilies in rice. We anticipate that the data provided here will serve as a foundation for targeted functional studies in rice and other plants. The application of yeast two-hybrid and TAPtag analyses for large-scale plant protein interaction studies is also discussed.

show abstract

Armadillo Repeat Proteins: Versatile Regulators of Plant Development and Signalling

Coates

Plant Cell Monographs

View full text Add to dashboard Cite

Multifunctional Arm Repeat Domains in Plants

Cited by 67 publications

References 110 publications

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

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

A Rice Kinase-Protein Interaction Map

Armadillo Repeat Proteins: Versatile Regulators of Plant Development and Signalling

Contact Info

Product

Resources

About