Wortmannin treatment induces changes in Arabidopsis root proteome and post-Golgi compartments
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22524784
DOI
10.1021/pr201111n
Knihovny.cz E-resources
- MeSH
- Androstadienes pharmacology MeSH
- Arabidopsis cytology drug effects metabolism MeSH
- Phospholipase D metabolism MeSH
- Plant Roots cytology drug effects metabolism MeSH
- Multivesicular Bodies drug effects metabolism MeSH
- Arabidopsis Proteins metabolism MeSH
- Phospholipid Transfer Proteins metabolism MeSH
- Proteome metabolism MeSH
- rab GTP-Binding Proteins metabolism MeSH
- trans-Golgi Network drug effects metabolism ultrastructure MeSH
- Protein Transport drug effects MeSH
- Wortmannin MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Androstadienes MeSH
- Phospholipase D MeSH
- phospholipase D1 MeSH Browser
- Arabidopsis Proteins MeSH
- Phospholipid Transfer Proteins MeSH
- Proteome MeSH
- rab GTP-Binding Proteins MeSH
- Wortmannin MeSH
Wortmannin is a widely used pharmaceutical compound which is employed to define vesicular trafficking routes of particular proteins or cellular compounds. It targets phosphatidylinositol 3-kinase and phosphatidylinositol 4-kinases in a dose-dependent manner leading to the inhibition of protein vacuolar sorting and endocytosis. Combined proteomics and cell biological approaches have been used in this study to explore the effects of wortmannin on Arabidopsis root cells, especially on proteome and endomembrane trafficking. On the subcellular level, wortmannin caused clustering, fusion, and swelling of trans-Golgi network (TGN) vesicles and multivesicular bodies (MVBs) leading to the formation of wortmannin-induced multivesicular compartments. Appearance of wortmannin-induced compartments was associated with depletion of TGN as revealed by electron microscopy. On the proteome level, wortmannin induced massive changes in protein abundance profiles. Wortmannin-sensitive proteins belonged to various functional classes. An inhibition of vacuolar trafficking by wortmannin was related to the downregulation of proteins targeted to the vacuole, as showed for vacuolar proteases. A small GTPase, RabA1d, which regulates vesicular trafficking at TGN, was identified as a new protein negatively affected by wortmannin. In addition, Sec14 was upregulated and PLD1 alpha was downregulated by wortmannin.
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