Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation

FEBS Lett. 1997 Dec 29;420(2-3):151-5. doi: 10.1016/s0014-5793(97)01506-8.

Abstract

Sucrose synthase (SuSy) plays an important role in sucrose degradation and occurs both as a soluble and as a membrane-associated enzyme in higher plants. We show that membrane association can vary in vivo in response to gravistimulation, apparently involving SuSy dephosphorylation, and is a reversible process in vitro. Phosphorylation of SuSy has little effect on its activity but decreases its surface hydrophobicity as reported with the fluorescent probe bis-ANS. We postulate that phosphorylation of SuSy (and perhaps other membrane proteins) is involved in the release of the membrane-bound enzyme in part as a result of decreased surface hydrophobicity.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Anilino Naphthalenesulfonates / metabolism
  • Blotting, Western
  • Cyclic AMP-Dependent Protein Kinases / antagonists & inhibitors
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Inhibitors / pharmacology
  • Fluorescent Dyes / metabolism
  • Glucosyltransferases / analysis
  • Glucosyltransferases / metabolism*
  • Gravitation
  • Membrane Proteins / metabolism
  • Phosphorylation
  • Plant Proteins / metabolism
  • Precipitin Tests
  • Solubility
  • Uridine Diphosphate Glucose / metabolism
  • Zea mays / enzymology*

Substances

  • Anilino Naphthalenesulfonates
  • Enzyme Inhibitors
  • Fluorescent Dyes
  • Membrane Proteins
  • Plant Proteins
  • 5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)
  • Adenosine Triphosphate
  • Glucosyltransferases
  • sucrose synthase
  • Cyclic AMP-Dependent Protein Kinases
  • Uridine Diphosphate Glucose