A serine involved in actin-dependent subcellular localization of a stress-induced tobacco BY-2 hydroxymethylglutaryl-CoA reductase isoform |
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Authors: | Merret Rémy Cirioni Jean- Roger Bach Thomas J Hemmerlin Andréa |
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Institution: | Institut de Biologie Moléculaire des Plantes CNRS-UPR 2357, Université Louis Pasteur, Département Isopréno?des, 28 Rue Goethe, F-67083 Strasbourg, France. |
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Abstract: | 3-Hydroxy-3-methylglutaryl-CoA reductase (HMGR) is unique in the first part of the cytoplasmic isoprenoid pathway, as it contains a membrane domain that includes ER-specific retention motifs. When fused to GFP, this domain targets two tobacco BY-2 HMGR isoforms differentially. While the first isoform is ER-localized, a second stress-induced one forms globular structures connected by tubular structures. A serine positioned upstream of the ER retention motif seems to be implicated in this specific subcellular localization. Surprisingly, these structures are closely connected to F-actin, and their intactness is dependent upon the integrity of the filaments or the action of a calmodulin antagonist. |
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Keywords: | CLSM confocal laser scanning microscopy ER endoplasmic reticulum GFP green fluorescent protein HMGR 3-hydroxy-3-methylglutaryl-CoA reductase MVA mevalonate RFP red fluorescent protein TBY-2 tobacco Bright Yellow 2 TMD trans-membrane domain WT wild-type |
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