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

FEBS Letters

Nielsen, Morten S.¹  Petersen, Claus M.¹  Gliemann, Jørgen¹  Smit, August B.²  Jacobsen, Linda²  Madsen, Peder¹  Geraerts, Wijnand P.M.² 

[1] Department of Medical Biochemistry, University of Aarhus, DK-8000 Aarhus C, Denmark;Department of Molecular and Cellular Neurobiology, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands

关键词: SorLA;    Sortilin;    GGA;    Sorting adaptor;    ac-LL;    acidic cluster-dileucine (motif);    cd;    cytoplasmic domain;    CD;    cation-dependent;    CI;    cation-independent;    GGA;    Golgi-localizing γ-adaptin ear homologous ADP-ribosylation factor (ARF)-binding protein;    GAEH;    γ-adaptin ear homology;    GST;    glutathione S-transferase;    IL2R;    interleukin 2 receptor-α (Tac;    CD25);    LDLR;    low density lipoprotein receptor;    MPR;    mannose 6-phosphate receptor;    TGN;    trans-Golgi network;    wt;    wild type;    VHS;    Vps27/Hrs/STAM homology;   

DOI  :  10.1016/S0014-5793(01)03299-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (Ψ–Ψ–X–X–∅) defining minimum requirements for GGA binding to cytoplasmic receptor domains.

【 授权许可】

Unknown