The sorLA cytoplasmic domain interacts with GGA1 and-2 and defines minimum requirements for GGA binding
The sorLA cytoplasmic domain interacts with GGA1 and-2 and defines minimum requirements for GGA binding
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DOI：
10.1016/s0014-5793(01)03299-9
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发表时间：
2002-01-30
期刊：
影响因子：
3.5
通讯作者：
Petersen, CM
中科院分区：
文献类型：
--
作者：
Jacobsen, L;Madsen, P;Petersen, CM
我们报告说，Vps 10 p结构域受体sorLA结合衔接蛋白GGA 1和-2，这参与高尔基体内体分选。GGA通过sorLA胞质尾的C-末端区段中的三个关键残基以不同的要求结合。与分拣蛋白和甘露糖6-磷酸受体不同，sorLA中的GGA结合片段既不含酸性簇也不含双亮氨酸。我们的研究结果支持的概念，sorLA作为一个潜在的分选受体，并表明，在sorLA和分拣蛋白的关键残基符合一种新型的基序（Psi-Psi-X-X-O）定义GGA结合到细胞质受体结构域的最低要求。(C)2002年欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (Psi-Psi-X-X-O) defining minimum requirements for GGA binding to cytoplasmic receptor domains. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.