FEBS Letters | |
The sorLA cytoplasmic domain interacts with GGA1 and ‐2 and defines minimum requirements for GGA binding | |
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
【 预 览 】
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RO201912020311398ZK.pdf | 231KB | download |