Expression of CLAVATA3 fusions indicates rapid intracellular processing and a role of ERAD

Marchis, Francesca De; Colanero, Sara; Klein, Eva M.; Mainieri, Davide; Prota, Viviana M.; Bellucci, Michele; Pagliuca, Giampiero; Zironi, Elisa; Gazzotti, Teresa; Vitale, Alessandro; Pompa, Andrea

doi:10.1016/j.plantsci.2018.03.020

Cited by 6 publications

(4 citation statements)

References 68 publications

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“…This finding illustrates a role for CDC48 in removing non-functional proteins. Other client proteins of CDC48 were identified such as the soluble secretory protein CLAVATA3 [37], the small GTPase ARF1 involved in subcellular trafficking [38], immune receptors [30] and proteins involved in various cellular processes (see the following sub-chapters for further details).…”

Section: -Introductionmentioning

confidence: 99%

Toward the understanding of the role of CDC48, a major component of the protein quality control, in plant immunity

et al. 2019

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The evolutionally conserved chaperone-like protein CDC48 (cell division cycle 48) is a major component of ubiquitin-dependent protein degradation pathways in animal and yeast and, more generally, of the protein quality control machinery. In plants, CDC48 plays essential regulatory functions in development and the possibly that it contributes to protein degradation through the ubiquitin-proteasome system (UPS) and the endoplasmic reticulum-associated protein degradation (ERAD) system has been reported. In this review we described recent findings highlighting a role for CDC48 in plant immunity. First data indicated that CDC48 is S-nitrosylated in plant cells undergoing an immune response, regulates the turnover of immune receptors and mediates the degradation of viral proteins.Furthermore its overexpression was associated to an exacerbated hypersensitive-like cell death. We also designed and reported here the first CDC48 interactome. The corresponding data confirms the closed interaction of CDC48 with components of the UPS and shed light on its putative regulatory function of S-adenosyl-methionine synthesis and metabolism. More generally, these investigations further support the concept that plant cells facing pathogen attack finely regulate the protein quality control machinery. Highlights-The chaperone-like protein CDC48 is a component of the ubiquitin-proteasome system -CDC48 contributes to the turnover of immune receptors -CDC48 is mobilized by cells facing an immune response -Overproduction of CDC48 leads to exacerbated cell death during the immune response -The A. thaliana CDC48 interactome highlights new functions of CDC48 Keywords

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Section: -Introductionmentioning

confidence: 99%

Toward the understanding of the role of CDC48, a major component of the protein quality control, in plant immunity

et al. 2019

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“…Immunoprecipitation experiments were performed in cells at the exponential phase grown in TAP medium under continuous light at 70 μmol photons m –2 sec –1 , as described by De Marchis et al. ( 2018 ) for Nicotiana tabacum (tobacco) protoplasts, with minor modifications. In brief, approximately 3 million algae cells were subjected to pulse labelling for up to 2 h by using Pro‐Mix – a mixture of [ 35 S]Met and [ 35 S]Cys (GE Healthcare, https://www.gehealthcare.com ).…”

Section: Methodsmentioning

confidence: 99%

LPA2 protein is involved in photosystem II assembly in Chlamydomonas reinhardtii

et al. 2021

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Photosynthetic eukaryotes require the proper assembly of photosystem II (PSII) in order to strip electrons from water and fuel carbon fixation reactions. In Arabidopsis thaliana, one of the PSII subunits (CP43/PsbC) was suggested to be assembled into the PSII complex via its interaction with an auxiliary protein called Low PSII Accumulation 2 (LPA2). However, the original articles describing the role of LPA2 in PSII assembly have been retracted. To investigate the function of LPA2 in the model organism for green algae, Chlamydomonas reinhardtii, we generated knockout lpa2 mutants by using the CRISPR-Cas9 target-specific genome editing system. Biochemical analyses revealed the thylakoidal localization of LPA2 protein in the wild type (WT), whereas lpa2 mutants were characterized by a drastic reduction in the levels of D1, D2, CP47 and CP43 proteins. Consequently, reduced PSII supercomplex accumulation, chlorophyll content per cell, PSII quantum yield and photosynthetic oxygen evolution were measured in the lpa2 mutants, leading to the almost complete impairment of photoautotrophic growth. Pulse-chase experiments demonstrated that the absence of LPA2 protein caused reduced PSII assembly and reduced PSII turnover. Taken together, our data indicate that, in C. reinhardtii, LPA2 is required for PSII assembly and proper function.

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“…Subcellular fractionation was performed by isopycnic gradient ultracentrifugation as described (De Marchis et al, 2018). Briefly, cells were homogenized with buffer without detergent (12% sucrose, ª 2020 The Authors EMBO Reports 21: e49756 | 2020 10 mM KCl, 2 mM MgCl 2 , 100 mM Tris-HCl, pH 7.8).…”

Section: Isopycnic Gradient Analysismentioning

confidence: 99%

“…Subcellular fractionation was performed by isopycnic gradient ultracentrifugation as described (De Marchis et al, 2018)…”

Section: Isopycnic Gradient Analysismentioning

confidence: 99%

Class IA PI3Ks regulate subcellular and functional dynamics of IDO1

et al. 2020

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Knowledge of a protein's spatial dynamics at the subcellular level is key to understanding its function(s), interactions, and associated intracellular events. Indoleamine 2,3-dioxygenase 1 (IDO1) is a cytosolic enzyme that controls immune responses via tryptophan metabolism, mainly through its enzymic activity. When phosphorylated, however, IDO1 acts as a signaling molecule in plasmacytoid dendritic cells (pDCs), thus activating genomic effects, ultimately leading to long-lasting immunosuppression. Whether the two activities-namely, the catalytic and signaling functions-are spatially segregated has been unclear. We found that, under conditions favoring signaling rather than catabolic events, IDO1 shifts from the cytosol to early endosomes. The event requires interaction with class IA phosphoinositide 3kinases (PI3Ks), which become activated, resulting in full expression of the immunoregulatory phenotype in vivo in pDCs as resulting from IDO1-dependent signaling events. Thus, IDO1's spatial dynamics meet the needs for short-acting as well as durable mechanisms of immune suppression, both under acute and chronic inflammatory conditions. These data expand the theoretical basis for an IDO1-centered therapy in inflammation and autoimmunity.

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Expression of CLAVATA3 fusions indicates rapid intracellular processing and a role of ERAD

Cited by 6 publications

References 68 publications

Toward the understanding of the role of CDC48, a major component of the protein quality control, in plant immunity

Toward the understanding of the role of CDC48, a major component of the protein quality control, in plant immunity

LPA2 protein is involved in photosystem II assembly in Chlamydomonas reinhardtii

Class IA PI3Ks regulate subcellular and functional dynamics of IDO1

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