Lentil seed aquaporins form a hetero-oligomer which is phosphorylated by a Mg(2+)-dependent and Ca(2+)-regulated kinase

Biochem J. 2000 Nov 15;352 Pt 1(Pt 1):183-90.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aquaporins / chemistry*
  • Autoradiography
  • Blotting, Western
  • Calcium / metabolism*
  • Cell Membrane / metabolism
  • Cross-Linking Reagents / pharmacology
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Fabaceae / chemistry*
  • Hydrogen-Ion Concentration
  • Ions
  • Magnesium / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Phosphorylation
  • Phosphotransferases / chemistry*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Plants, Medicinal*
  • Protein Binding
  • Protein Conformation
  • Protein Isoforms
  • Protein Kinases / chemistry*
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid
  • Temperature
  • Time Factors

Substances

  • Aquaporins
  • Cross-Linking Reagents
  • Ions
  • Membrane Proteins
  • Plant Proteins
  • Protein Isoforms
  • tonoplast intrinsic protein, plant
  • Phosphotransferases
  • Protein Kinases
  • Magnesium
  • Calcium