Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism

被引:56
作者
Kato, Y
Misra, S
Puertollano, R
Hurley, JH [1 ]
Bonifacino, JS
机构
[1] NIDDKD, Mol Biol Lab, NIH, Bethesda, MD 20892 USA
[2] NICHHD, Cell Biol & Metab Branch, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1038/nsb807
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
Phosphorylation of the cytosolic tails of transmembrane receptors can regulate their intracellular trafficking. The structural basis for such regulation, however, has not been explained in most cases. The cytosolic tail of the cation-independent mannose 6-phosphate receptor contains a serine residue within an acidic-cluster dileucine signal that is important for the function of the receptor in the biosynthetic sorting of lysosomal hydrolases. We show here that phosphorylation of this Ser enhances interactions of the signal with its recognition module, the VHS domain of the GGA proteins. Crystallographic analyses demonstrate that the phosphoserine residue interacts electrostatically with two basic residues on the VHS domain of GGA3, thus providing an additional point of attachment of the acidic-cluster dileucine signal to its recognition module.
引用
收藏
页码:532 / 536
页数:5
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