Cullins 3a and 3b Assemble with Members of the Broad Complex/Tramtrack/Bric-a-Brac (BTB) Protein Family to Form Essential Ubiquitin-Protein Ligases (E3s) in Arabidopsis

Gingerich, Derek J.; Gagne, Jennifer M.; Salter, Donald W.; Hellmann, Hanjo; Estelle, Mark; Ma, Ligeng; Vierstra, Richard D.

doi:10.1074/jbc.m413247200

Cited by 155 publications

(194 citation statements)

References 71 publications

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“…A sequence similarity search in the Arabidopsis genome revealed the presence of at least 11 predicted CULLIN-related genes [42][43][44] (Supplementary Table S1). However, intact canonical C-and Nterminal domains were retrieved only for six CULLIN proteins, whereas four conserve only the N-terminal domain.…”

Section: The Cullin Familymentioning

confidence: 99%

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

Mazzucotelli

Belloni²,

Marone³

et al. 2006

241

178

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Abstract:The regulation of protein expression and activity has been for long time considered only in terms of transcription/translation efficiency. In the last years, the discovery of post-transcriptional and post-translational regulation mechanisms pointed out that the key factor in determining transcript/protein amount is the synthesis/degradation ratio, together with post-translational modifications of proteins. Polyubiquitinaytion marks target proteins directed to degradation mediated by 26S-proteasome. Recent functional genomics studies pointed out that about 5% of Arabidopsis genome codes for proteins of ubiquitination pathway. The most of them (more than one thousand genes) correspond to E3 ubiquitin ligases that specifically recognise target proteins. The huge size of this gene family, whose members are involved in regulation of a number of biological processes including hormonal control of vegetative growth, plant reproduction, light response, biotic and abiotic stress tolerance and DNA repair, indicates a major role for protein degradation in control of plant life.

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Section: The Cullin Familymentioning

confidence: 99%

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

Mazzucotelli

Belloni²,

Marone³

et al. 2006

241

178

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“…Our study unravels a specific requirement of a BTB/POZdomain protein for PEN3 membrane trafficking. The BTB/POZdomain is an evolutionarily conserved motif and protein-protein interaction domain found in proteins involved in a wide range of cellular functions [13][14][15][16][17] . The Arabidopsis genome encodes for around 80 BTB/POZ-domain proteins, of which a small subset act as substrate adaptors for E3 ubiquitin ligase complexes by interacting with CULLIN3 (CUL3) [13][14][15][16] .…”

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confidence: 99%

“…The BTB/POZdomain is an evolutionarily conserved motif and protein-protein interaction domain found in proteins involved in a wide range of cellular functions [13][14][15][16][17] . The Arabidopsis genome encodes for around 80 BTB/POZ-domain proteins, of which a small subset act as substrate adaptors for E3 ubiquitin ligase complexes by interacting with CULLIN3 (CUL3) [13][14][15][16] . Whereas no BTB/POZ-domain protein has previously been associated with ER membrane trafficking in plants, a precedent exists in mammals: Transport of procollagen I from the ER involves monoubiquitylation-dependent regulation of the COPII component SEC31, which requires the KLHL12 BTB/ POZ-domain protein as a CUL3 adaptor 13,17,18 .…”

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confidence: 99%

“…However, KLHL12 and EAP3 are molecularly unrelated except for harbouring a BTB/ POZ domain. Moreover, the BTB/POZ domain of EAP3 displays poor conservation of the residues required for CUL3 binding and is not likely to function as an E3 ligase adaptor 15,16 . Thus, we hypothesize that EAP3 mediates protein-protein interactions at the cytosolic face of the ER, where the ATP-binding cassette domains of PEN3 are located 1 .…”

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Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficking and disease susceptibility

et al. 2017

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The outermost cell layer of plant roots (epidermis) constantly encounters environmental challenges. The epidermal outer plasma membrane domain harbours the PENETRATION3 (PEN3)/ABCG36/PDR8 ATP-binding cassette transporter that confers non-host resistance to several pathogens. Here, we show that the Arabidopsis ENDOPLASMIC RETICULUM-ARRESTED PEN3 (EAP3) BTB/POZ-domain protein specifically mediates PEN3 exit from the endoplasmic reticulum and confers resistance to a root-penetrating fungus, providing prime evidence for BTB/POZ-domain protein-dependent membrane trafficking underlying disease resistance.The PENETRATION3 (PEN3/ABCG36/PDR8) ATP-binding cassette transporter of Arabidopsis thaliana is a crucial component of preinvasive defence against some fungal and bacterial nonhost pathogens entering by direct penetration 1-4 . In above-ground organs, PEN3 is recruited to sites of pathogen attack at the cell surface 3,4 . In seedling roots, PEN3 polarly localizes to the epidermal outer membrane domain in the absence of pathogens 5,6 . Root epidermal cells display four major polar plasma membrane domains: the outer domain facing the environment, the inner domain oriented towards the cortical cell layer, the shootward-oriented, apical, and the root tip-oriented, basal, domain 6 . Proteins in the outer domain that function in regulating the transport of inorganic compounds include, for example, the NIP5;1 boric acid uptake channel 7 . Factors required for PEN3 and NIP5;1 trafficking from the transGolgi network to the outer domain have been identified [8][9][10] , and exocyst complex components promote polar tethering of several outer domain proteins 9,11 . However, factors that specifically mediate trafficking of polar outer membrane cargos involved in responses to root-penetrating pathogens remain to be discovered.In a genetic screen for mislocalization of PEN3 fused to greenfluorescent protein (PEN3-GFP) in the root epidermis of seedlings 9 , we recovered one recessive mutant in which PEN3-GFP localized to a cytoplasmic structure resembling the endoplasmic reticulum (ER) (Fig. 1a-d). This er-arrested pen3-1 (eap3-1) mutation indistinguishably affected localization of PEN3-GFP from that of PEN3-mCherry ( Supplementary Fig. 1a,b), which colocalized with the ER-intrinsic chaperone BIP in the eap3-1 mutant ( Supplementary Fig. 1c,d), corroborating an ER arrest of PEN3.We mapped the eap3-1 mutation to a 275-kb interval on chromosome 3 by recombination mapping (Fig. 1e) combined with mapping and mutation identification by deep sequencing. This interval contained one non-synonymous, single-nucleotide polymorphism that caused a G to A missense mutation resulting in the conversion of glycine 192 to glutamate (eap3 G192E ) in the predicted open reading frame of gene model At3g09030.1 (Fig. 1f). Wild type and homozygous eap3-1 mutants displayed similar EAP3 transcript levels ( Fig. 1g), whereas the SALK_101331 T-DNA insertion located in the single exon of At3g09030 (designated eap3-2) caused a lack of full-length EAP3 messenger ...

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“…Arabidopsis expresses four functionally relevant cullins giving rise to three distinct classes of CRLs. The functionally redundant cullins CUL3A and CUL3B associate with BTB/POZ (Bric-a-brac, Tramtrack, and broad complex/Pox virus and zinc finger) domain-containing substrate adaptors (5)(6)(7). CUL4 associates with a subgroup of WD40 repeat-containing proteins called DWD proteins via the DDB1 adaptor (8,9).…”

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confidence: 99%

COP9 Signalosome- and 26S Proteasome-dependent Regulation of SCFTIR1 Accumulation in Arabidopsis

Stuttmann

Lechner

Guérois

et al. 2009

Journal of Biological Chemistry

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Ubiquitination and proteasome-mediated degradation of proteins are crucial for eukaryotic physiology and development. The largest class of E3 ubiquitin ligases is made up of the cullin-RING ligases (CRLs), which themselves are positively regulated through conjugation of the ubiquitin-like peptide RUB/NEDD8 to cullins. RUB modification is antagonized by the COP9 signalosome (CSN), an evolutionarily conserved eight-subunit complex that is essential in most eukaryotes and cleaves RUB from cullins. The CSN behaves genetically as an activator of CRLs, although it abolishes CRL activity in vitro. This apparent paradox was recently reconciled in different organisms, as the CSN was shown to prevent autocatalytic degradation of several CRL substrate adaptors. We tested for such a mechanism in the model plant Arabidopsis by measuring the impact of a newly identified viable csn2 mutant on the activity and stability of SCF TIR1 , a receptor to the phytohormone auxin and probably the best characterized plant CRL. Our analysis reveals that not only the F-box protein TIR1 but also relevant cullins are destabilized in csn2 and other Arabidopsis csn mutants. These results provide an explanation for the auxin resistance of csn mutants. We further observed in vivo a post-translational modification of TIR1 dependent on the proteasome inhibitor MG-132 and provide evidence for proteasome-mediated degradation of TIR1, CUL1, and ASK1 (Arabidopsis SKP1 homolog). These results are consistent with CSN-dependent protection of Arabidopsis CRLs from autocatalytic degradation, as observed in other eukaryotes, and provide evidence for antagonist roles of the CSN and 26S proteasome in modulating accumulation of the plant CRL SCF TIR1 .

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Cullins 3a and 3b Assemble with Members of the Broad Complex/Tramtrack/Bric-a-Brac (BTB) Protein Family to Form Essential Ubiquitin-Protein Ligases (E3s) in Arabidopsis

Cited by 155 publications

References 71 publications

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficking and disease susceptibility

COP9 Signalosome- and 26S Proteasome-dependent Regulation of SCFTIR1 Accumulation in Arabidopsis

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