PMID:11397085

Citation	Shah, K, Gadella, TW Jr, van Erp, H, Hecht, V and de Vries, SC (2001) Subcellular localization and oligomerization of the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 protein. J. Mol. Biol. 309:641-55
Abstract	The Arabidopsis thaliana somatic embryogenesis receptor kinase 1 (AtSERK1) gene is expressed in developing ovules and early embryos. AtSERK1 is also transiently expressed during somatic embryogenesis. The predicted AtSERK1 protein contains an extracellular domain with a leucine zipper motif followed by five leucine-rich repeats, a proline-rich region, a single transmembrane region and an intracellular kinase domain. The AtSERK1 cDNA was fused to two different variants of green fluorescent protein (GFP), a yellow-emitting GFP (YFP) and a cyan-emitting GFP (CFP), and transiently expressed in both plant protoplasts and insect cells. Using confocal laser scanning microscopy it was determined that the AtSERK1-YFP fusion protein is targeted to plasma membranes in both plant and animal cells. The extracellular leucine-rich repeats, and in particular the N-linked oligosaccharides that are present on them appear to be essential for correct localization of the AtSERK1-YFP protein. The potential for dimerization of the AtSERK1 protein was investigated by measuring the YFP/CFP fluorescence emission ratio using fluorescence spectral imaging microscopy. This ratio will increase due to fluorescence resonance energy transfer if the AtSERK1-CFP and AtSERK1-YFP fusion proteins interact. In 15 % of the cells the YFP/CFP emission ratio for plasma membrane localized AtSERK1 proteins was enhanced. Yeast-protein interaction experiments confirmed the possibility for AtSERK1 homodimerization. Elimination of the extracellular leucine zipper domain reduced the YFP/CFP emission ratio to control levels indicating that without the leucine zipper domain AtSERK1 is monomeric.
Links	PubMed Online version:10.1006/jmbi.2001.4706
Keywords	Amino Acid Motifs; Animals; Arabidopsis/cytology; Arabidopsis/drug effects; Arabidopsis/enzymology; Arabidopsis/metabolism; Cell Line; Cell Membrane/metabolism; Dimerization; Energy Transfer; Fluorescence; Glycosylation; Leucine Zippers; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Mitogen-Activated Protein Kinase Kinases/chemistry; Mitogen-Activated Protein Kinase Kinases/metabolism; Plant Proteins/chemistry; Plant Proteins/metabolism; Protein Binding; Protein Structure, Tertiary; Protein Transport; Protoplasts/cytology; Protoplasts/metabolism; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/metabolism; Spectrometry, Fluorescence; Spodoptera; Tunicamycin/pharmacology; Two-Hybrid System Techniques
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