Premium
Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation
Author(s) -
Winter Heike,
Huber Joan L,
Huber Steven C
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01506-8
Subject(s) - dephosphorylation , phosphorylation , atp synthase , enzyme , membrane , biochemistry , sucrose , sucrose synthase , chemistry , biophysics , membrane protein , protein phosphorylation , biology , microbiology and biotechnology , phosphatase , protein kinase a , invertase
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.