RRC ID 29125
著者 Herberth S, Shahriari M, Bruderek M, Hessner F, Müller B, Hülskamp M, Schellmann S.
タイトル Artificial ubiquitylation is sufficient for sorting of a plasma membrane ATPase to the vacuolar lumen of Arabidopsis cells.
ジャーナル Planta
Abstract Sorting of transmembrane proteins into the inner vesicles of multivesicular bodies for subsequent delivery to the vacuole/lysosome can be induced by attachment of a single ubiquitin or K63-linked ubiquitin chains to the cytosolic portion of the cargo in yeast and mammals. In plants, large efforts have been undertaken to elucidate the mechanisms of vacuolar trafficking of soluble proteins. Sorting of transmembrane proteins, by contrast, is still largely unexplored. As a proof of principle, that ubiquitin is involved in vacuolar sorting in plants we show that a translational fusion of a single ubiquitin to the Arabidopsis plasma membrane ATPase PMA-EGFP is sufficient to induce its endocytosis and sorting into the vacuolar lumen. Sorting of the artificial reporter is not dependent on ubiquitin chain formation, but involves ubiquitin's hydrophobic patch and can be inhibited by coexpression of a dominant-negative version of the ESCRT (endosomal sorting complex required for transport) related protein AtSKD1 (SUPPRESSOR OF K+ TRANSPORT GROWTH DEFECT1). Our results suggest that ubiquitin can in principle act as vacuolar sorting signal in plants.
巻・号 236(1)
ページ 63-77
公開日 2012-7-1
DOI 10.1007/s00425-012-1587-0
PMID 22258747
MeSH Adenosine Triphosphatases / metabolism* Arabidopsis / metabolism* Cell Membrane / enzymology* Endosomal Sorting Complexes Required for Transport / metabolism Protein Transport / physiology* Signal Transduction Ubiquitin / metabolism* Ubiquitinated Proteins / metabolism* Ubiquitination Vacuoles / physiology*
IF 3.39
引用数 28
WOS 分野 PLANT SCIENCES
リソース情報
シロイヌナズナ / 植物培養細胞・遺伝子 pda01520 pda13191