sorLA胞质结构域与GGA1和-2相互作用，并确定了GGA结合的最低要求。

The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.

作者信息

Jacobsen Linda, Madsen Peder, Nielsen Morten S, Geraerts Wijnand P M, Gliemann Jørgen, Smit August B, Petersen Claus M

机构信息

Department of Molecular and Cellular Neurobiology, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands.

出版信息

FEBS Lett. 2002 Jan 30;511(1-3):155-8. doi: 10.1016/s0014-5793(01)03299-9.

DOI:10.1016/s0014-5793(01)03299-9

PMID:11821067

Abstract

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-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.

摘要

我们报道Vps10p结构域受体sorLA与参与高尔基体-内体分选的衔接蛋白GGA1和GGA2结合。GGA蛋白通过sorLA细胞质尾部C末端片段中的三个关键残基以不同的要求进行结合。与sortilin和甘露糖6-磷酸受体不同，sorLA中的GGA结合片段既不包含酸性簇也不包含双亮氨酸。我们的结果支持sorLA作为潜在分选受体的概念，并表明sorLA和sortilin中的关键残基符合一种新型基序（ψ-ψ-X-X-φ），该基序定义了GGA与细胞质受体结构域结合的最低要求。