The carboxy‐terminal domain of the receptor‐associated protein binds to the Vps10p domain of sortilin

FEBS Letters

Jacobsen, Christian¹  Thøgersen, Hans C²  Petersen, Claus Munck¹  Moestrup, Søren K¹  Gliemann, Jørgen¹  Ellgaard, Lars²  Tauris, Jacob¹  Nielsen, Morten S¹  Madsen, Peder¹ 

[1] Department of Medical Biochemistry, University of Aarhus, 8000 Aarhus C, Denmark;Laboratory of Gene Expression, University of Aarhus, 8000 Aarhus C, Denmark

关键词: Sortilin;    Receptor-associated protein;    Chaperone;    Sorting;    Brain;   

DOI  :  10.1016/S0014-5793(98)00559-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Binding of the receptor-associated protein (RAP) to the newly identified putative sorting receptor, sortilin, was analyzed by surface plasmon resonance analysis of recombinant RAP and sortilin domains and compared with binding to megalin and low density lipoprotein receptor-related protein (LRP). The data show that the RAP-binding site in sortilin is localized in the cysteine-rich lumenal part homologous to yeast vacuolar protein-sorting 10 protein (Vps10p), and the sortilin-binding site in RAP is localized in the carboxy-terminal domain III of the three homologous domains in RAP. Whereas sortilin bound only RAP domain III, megalin and LRP bound all RAP domains with the functional affinity order: domain III>domain I>domain II.

【 授权许可】

Unknown