Phosphorylation-independent interaction between 14-3-3 protein and the plant plasma membrane H+-ATPase

被引：20

作者：

Borch, J

Bych, K

Roepstorff, P

Palmgren, MG

Fuglsang, AT

机构：

[1] Royal Vet & Agr Univ, Plant Physiol & Anat Lab, Dept Plant Biol, DK-1871 Frederiksberg C, Denmark

[2] Univ Denmark So, Dept Biochem & Mol Biol, DK-5230 Odense, Denmark

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2002年 / 30卷

关键词：

binding motif; fusicoccin;

D O I：

10.1042/bst0300411

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

14-3-3 proteins interact with a novel phosphothreonine motif (Y(946)pTV) at the extreme C-terminal end of the plant plasma membrane H+-ATPase molecule. Phosphorylation-independent binding of 14-3-3 protein to the YTV motif can be induced by the fungal phytotoxin fusicoccin. The molecular basis for the phosphorylation-independent interaction between 14-3-3 and H+-ATPase in the presence of fusicoccin has been investigated in more detail. Fusicoccin binds to a heteromeric receptor that involves both 14-3-3 protein and H+-ATPase. Binding of fusicoccin is dependent upon the YTV motif in the H+-ATPase and, in addition, requires residues further upstream of this motif. Apparently, 14-3-3 proteins interact with the unusual epitope in H+-ATPase via its conserved amphipathic groove. This implies that very diverse epitopes bind to a common structure in the 14-3-3 protein.

引用

收藏

页码：411 / 415

页数：5

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