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Published on: March 18, 2011
Sphingolipids involvement in plant endomembrane differentiation: the BY2 case.
Anne Aubert1, Jessica Marion, Claire Boulogne
1Laboratoire Dynamique de la Compartimentation Cellulaire, CNRS UPR2355/IFR87, Institut des Sciences du Végétal, Centre de Recherche de Gif (FRC3115), 91198, Gif-sur-Yvette Cedex, France.
The Plant Journal : for Cell and Molecular Biology
|January 6, 2011
Summary
Fumonisin B1 (FB1) disrupts sphingolipid synthesis in plant cells, impacting growth, shape, and cell division. This highlights sphingolipids
Area of Science:
- Plant Cell Biology
- Molecular Plant Physiology
- Biochemistry
Background:
- Sphingolipids are crucial for the secretory pathway in eukaryotes.
- Their role in plant cell organization remains understudied.
- Fumonisin B1 (FB1) specifically inhibits ceramide synthase, a key enzyme in sphingolipid biosynthesis.
Purpose of the Study:
- To investigate the effects of FB1 on plant cell growth, polarity, shape, cell cycle, and secretory pathway ultrastructure.
- To elucidate the role of sphingolipids in the functional organization of plant cells.
Main Methods:
- Utilized BY2 cell lines with GFP-tagged organelle markers and a Golgi marker fused to Kaede.
- Employed light and electron microscopy, alongside flow cytometry, to analyze secretory pathway dynamics.
- Assessed cell growth, shape, cell cycle progression, and cargo transport inhibition.
Main Results:
- FB1 treatment severely affected cell growth and shape, delaying cell division.
- Observed formation of ER-derived tubular aggregates (FB1-induced compartments) and inhibited ER-to-Golgi transport.
- Noted altered polar localization of the auxin transporter PIN1, with minimal impact on endocytosis.
Conclusions:
- Inhibition of ceramide biosynthesis by FB1 profoundly impacts plant cell growth and polarity establishment.
- Sphingolipids are vital for the functional organization and compartmentalization of the endoplasmic reticulum in plant cells.
- FB1 targets distinct molecular pathways compared to brefeldin A (BFA).
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