The plant nuclear envelope protein MAF1 has an additional location at the Golgi and binds to a novel Golgi-associated coiled-coil protein |
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Authors: | Shalaka?Patel Jelena?Brkljacic Frank?Gindullis Annkatrin?Rose Email author" target="_blank">Iris?MeierEmail author |
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Institution: | (1) Plant Biotechnology Center and Department of Plant Cellular and Molecular Biology, The Ohio State University, 244 Rightmire Hall, 1060 Carmack Road, Columbus, OH 43210-1002, USA;(2) Present address: CellTec Biotechnology GmBF, Frohmestrasse 110, 22459 Hamburg, Germany |
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Abstract: | Tomato MAF1 (LeMAF1) is a plant-specific, nuclear envelope (NE)-associated protein. It is the founding member of a group of
WPP domain-containing, NE-associated proteins. This group includes the Arabidopsis WPP family, which is involved in cell division,
as well as plant RanGAPs. In addition to its NE localization, LeMAF1 accumulates in speckles in the cytoplasm. Here, we show
that the LeMAF1-containing speckles are components of the Golgi apparatus. A novel tomato coiled-coil protein was identified
that specifically binds to LeMAF1. Tomato WPP domain-associated protein (LeWAP) interacts in yeast and in vitro through its
coiled-coil domain with several WPP-domain containing proteins, including AtRanGAP1 and the WPP family (LeMAF, WPP1 and WPP2).
Like LeMAF1, LeWAP is localized at the Golgi. Moreover, we present data showing that Arabidopsis WAP is necessary for the
existence of a multi-protein complex containing WPP2.
Electronic Supplementary Material Supplementary material is available for this article at . |
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Keywords: | WPP domain WAP MAF1 Coiled-coil Golgi Golgin Blue-native gel electrophoresis |
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