14-3-3蛋白与植物质膜H⁺-ATP酶之间的非磷酸化依赖性相互作用。
Phosphorylation-independent interaction between 14-3-3 protein and the plant plasma membrane H+-ATPase.
作者信息
Borch J, Bych K, Roepstorff P, Palmgren M G, Fuglsang A T
机构信息
Department of Plant Biology, Plant Physiology and Anatomy Laboratory, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871-Frederiksberg C, Copenhagen, Denmark.
出版信息
Biochem Soc Trans. 2002 Aug;30(4):411-5. doi: 10.1042/bst0300411.
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.
14-3-3蛋白与植物质膜H(+) -ATP酶分子极端C末端的一个新的磷酸苏氨酸基序（Y(946)pTV）相互作用。真菌植物毒素壳梭孢菌素可诱导14-3-3蛋白与YTV基序的非磷酸化依赖性结合。已更详细地研究了在存在壳梭孢菌素的情况下14-3-3与H(+) -ATP酶之间非磷酸化依赖性相互作用的分子基础。壳梭孢菌素与一种异源受体结合，该受体涉及14-3-3蛋白和H(+) -ATP酶。壳梭孢菌素的结合取决于H(+) -ATP酶中的YTV基序，此外，还需要该基序上游的其他残基。显然，14-3-3蛋白通过其保守的两亲性凹槽与H(+) -ATP酶中不寻常的表位相互作用。这意味着非常多样的表位与14-3-3蛋白中的一个共同结构结合。
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