Molecular Genetics of the Ubiquitin-Proteasome System: Lessons from Yeast

Hochstrasser, Mark; Deng, Min; Kusmierczyk, Andrew R.; Li, X.; Kreft, Stefan G.; Ravid, Tommer; Funakoshi, Mitsuaki; Kunjappu, Mary J; Xie, Yang

doi:10.1007/2789_2008_100

Cited by 6 publications

(3 citation statements)

References 58 publications

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“…These domains are short and cannot be easily identified in silico due to a lack of sequence conservation and because the attachment of ubiquitin to substrates may not be restricted to Lys residues (Dreher et al, 2006;Hochstrasser et al, 2008). In fact, we have very poor knowledge of ubiquitylation sites on substrates altogether, even for well-studied proteins like the Aux/IAAs.…”

Section: Future Directionsmentioning

confidence: 99%

Ubiquitin-Mediated Control of Plant Hormone Signaling

2012

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Section: Future Directionsmentioning

confidence: 99%

Ubiquitin-Mediated Control of Plant Hormone Signaling

2012

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“…After an enzymatic cascade covalently attaches a polymer(s) of ubiquitin to a substrate protein, the substrate is targeted for degradation by the proteasome [1]. The mechanisms of ubiquitylation have been well studied, and are reviewed elsewhere [1, 5-8]. …”

Section: Introductionmentioning

confidence: 99%

Assembly of the 20S proteasome

Kunjappu

Hochstrasser

2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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The proteasome is a cellular protease responsible for the selective degradation of the majority of the intracellular proteome. It recognizes, unfolds, and cleaves proteins that are destined for removal, usually by prior attachment to polymers of ubiquitin. This macromolecular machine is composed of two subcomplexes, the 19S regulatory particle (RP) and the 20S core particle (CP), which together contain at least 33 different and precisely positioned subunits. How these subunits assemble into functional complexes is an area of active exploration. Here we describe the current status of studies on the assembly of the 20S proteasome (CP). The 28-subunit CP is found in all three domains of life and its cylindrical stack of four heptameric rings is well conserved. Though several CP subunits possess self-assembly properties, a consistent theme in recent years has been the need for dedicated assembly chaperones that promote on-pathway assembly. To date, a minimum of three accessory factors have been implicated in aiding the construction of the 20S proteasome. These chaperones interact with different assembling proteasomal precursors and usher subunits into specific slots in the growing structure. This review will focus largely on chaperone-dependent CP assembly and its regulation.

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“…Usually, ubiquitin ligase E3 can specifically recognize target proteins and is therefore particularly important and extensively studied. Ubiquitination is involved in various mechanisms including cell cycle, apoptosis, protein degradation, and immune regulation, and is, therefore, one of the most important mechanisms regulating various life activities (Smalle and Vierstra, 2004;Hochstrasser et al, 2008;Kim et al, 2010;Ulrich & Walden, 2010). The P. brassicae e3 genome contains 139 putative E3 ubiquitin ligases, among which 115 harbor the conserved RING domain.…”

Section: Introductionmentioning

confidence: 99%

The protist ubiquitin ligase effector PbE3-2 targets RD21A to impede plant immunity

Chen

Luo

et al. 2022

Preprint

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Clubroot caused by the soil-borne protist pathogen Plasmodiophora brassicae is one of the most devastating diseases of Brassica oil and vegetable crops worldwide. Understanding the pathogen infection strategy is crucial for the development of disease control. However, the molecular mechanism by which this pathogen promotes infection remains largely unknown. Here, we identified a P. brassicae-secreted effector PbE3-2 that impedes plant immunity by ubiquitinating the immune regulator RD21A for degradation. Overexpression of PbE3-2 in Arabidopsis thaliana resulted in higher susceptibility to P. brassicae and decreases in chitin-triggered reactive oxygen species burst and expression of marker genes in salicylic acid signaling. PbE3-2 interacted with and ubiquitinated RD21A in vitro and in vivo. Mutant plants deficient in RD21A exhibited similar susceptibility and compromsied immune responses as in PbE3-2 overexpression plants. These results suggest that P. brassicae promotes clubroot disease through RD21A degradation mediated by the effector PbE3-2. As PbE3-2 is widely conserved across different P. brassicae pathotypes, the degradation of RD21A by PbE3-2 might be a prevalent infection strategy in this pathogen.

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Molecular Genetics of the Ubiquitin-Proteasome System: Lessons from Yeast

Cited by 6 publications

References 58 publications

Ubiquitin-Mediated Control of Plant Hormone Signaling

Ubiquitin-Mediated Control of Plant Hormone Signaling

Assembly of the 20S proteasome

The protist ubiquitin ligase effector PbE3-2 targets RD21A to impede plant immunity

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