Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1896834#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B222133.
- aggregation creator B222134.
- aggregation creator B222135.
- aggregation creator B222136.
- aggregation creator B222137.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1896834.bibtex.
- aggregation hasFormat 1896834.csv.
- aggregation hasFormat 1896834.dc.
- aggregation hasFormat 1896834.didl.
- aggregation hasFormat 1896834.doc.
- aggregation hasFormat 1896834.json.
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- aggregation hasFormat 1896834.txt.
- aggregation hasFormat 1896834.xls.
- aggregation hasFormat 1896834.yaml.
- aggregation isPartOf urn:issn:0027-8424.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Monoubiquitin-dependent endocytosis of the Iron-Regulated Transporter 1 (IRT1) transporter controls iron uptake in plants".
- aggregation abstract "Plants take up iron from the soil using the IRON-REGULATED TRANSPORTER 1 (IRT1) high-affinity iron transporter at the root surface. Sophisticated regulatory mechanisms allow plants to tightly control the levels of IRT1, ensuring optimal absorption of essential but toxic iron. Here, we demonstrate that overexpression of Arabidopsis thaliana IRT1 leads to constitutive IRT1 protein accumulation, metal overload, and oxidative stress. IRT1 is unexpectedly found in trans-Golgi network/early endosomes of root hair cells, and its levels and localization are unaffected by iron nutrition. Using pharmacological approaches, we show that IRT1 cycles to the plasma membrane to perform iron and metal uptake at the cell surface and is sent to the vacuole for proper turnover. We also prove that IRT1 is monoubiquitinated on several cytosol-exposed residues in vivo and that mutation of two putative monoubiquitination target residues in IRT1 triggers stabilization at the plasma membrane and leads to extreme lethality. Together, these data suggest a model in which monoubiquitin-dependent internalization/sorting and turnover keep the plasma membrane pool of IRT1 low to ensure proper iron uptake and to prevent metal toxicity. More generally, our work demonstrates the existence of monoubiquitin-dependent trafficking to lytic vacuoles in plants and points to proteasome-independent turnover of plasma membrane proteins.".
- aggregation authorList BK487057.
- aggregation endPage "E458".
- aggregation issue "32".
- aggregation startPage "E450".
- aggregation volume "108".
- aggregation aggregates 1896920.
- aggregation isDescribedBy 1896834.
- aggregation similarTo pnas.1100659108.
- aggregation similarTo LU-1896834.