Internalized and Newly Synthesized Arabidopsis PIN- FORMED2 Pass through Brefeldin A Compartments: A New Insight into Intracellular Dynamics of the Protein by Using the Photoconvertible Fluorescence Protein Dendra2 as a Tag  被引量:1

Internalized and Newly Synthesized Arabidopsis PIN- FORMED2 Pass through Brefeldin A Compartments: A New Insight into Intracellular Dynamics of the Protein by Using the Photoconvertible Fluorescence Protein Dendra2 as a Tag

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作  者:Jan Jasik Elmon Schmelzer 

机构地区:[1]Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, 50829, Koln, Germany [2]Department of Botany, Revova 39, Faculty of Natural Sciences, Comenius University, 811 02 Bratislava 1, Slovakia [3]Department of Molecular Biology, Mlynská dolina, pavilion B-2, Faculty of Natural Sciences, Comenius University, 842 15 Bratislava 4, Slovakia

出  处:《Molecular Plant》2014年第10期1578-1581,共4页分子植物(英文版)

摘  要:Dear Editor, Plasma membrane (PM)-Iocalized PIN-FORMED (PIN) auxin efflux carriers were shown to cycle rapidly and con- tinuously between PM and the endomembrane system and this cycling is affected by many exogenous factors and endogenous programs (Grunewald and Friml, 2010). The fungal lactone metabolite Brefeldin A (BFA) is believed to interrupt the continuous cycling of PINs and other PM proteins by inhibiting their re-secretion (Kleine-Vehn and Friml, 2008).Dear Editor, Plasma membrane (PM)-Iocalized PIN-FORMED (PIN) auxin efflux carriers were shown to cycle rapidly and con- tinuously between PM and the endomembrane system and this cycling is affected by many exogenous factors and endogenous programs (Grunewald and Friml, 2010). The fungal lactone metabolite Brefeldin A (BFA) is believed to interrupt the continuous cycling of PINs and other PM proteins by inhibiting their re-secretion (Kleine-Vehn and Friml, 2008).

分 类 号:Q51[生物学—生物化学] TQ465[化学工程—制药化工]

 

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