Abstract
In plants, aquaporins regulate the water flow through membranes during growth, development and stress responses. We have isolated two isoforms of the aquaporin family from the protein-storage vacuoles of lentil (Lens culinaris Med.) seeds. Chemical cross-linking experiments showed that both isoforms belong to the same oligomer in the membrane and are phosphorylated by a membrane-bound protein kinase. We assigned the kinase activity to a 52 kDa protein that is magnesium-dependent and calcium-regulated.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Aquaporins / chemistry*
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Autoradiography
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Blotting, Western
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Calcium / metabolism*
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Cell Membrane / metabolism
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Cross-Linking Reagents / pharmacology
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Dose-Response Relationship, Drug
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Electrophoresis, Polyacrylamide Gel
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Fabaceae / chemistry*
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Hydrogen-Ion Concentration
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Ions
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Magnesium / metabolism*
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Molecular Sequence Data
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Phosphorylation
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Phosphotransferases / chemistry*
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Plant Proteins / chemistry
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Plant Proteins / metabolism
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Plants, Medicinal*
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Protein Binding
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Protein Conformation
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Protein Isoforms
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Protein Kinases / chemistry*
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Sequence Analysis, Protein
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Sequence Homology, Amino Acid
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Temperature
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Time Factors
Substances
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Aquaporins
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Cross-Linking Reagents
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Ions
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Membrane Proteins
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Plant Proteins
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Protein Isoforms
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tonoplast intrinsic protein, plant
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Phosphotransferases
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Protein Kinases
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Magnesium
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Calcium