Distinct in vitro interaction pattern of dopamine receptor subtypes with adaptor proteins involved in post‐endocytotic receptor targeting

FEBS Letters

Heydorn, Arne²  Holst, Birgitte²  Schwartz, Thue W²  Haft, Carol Renfrew¹  Søndergaard, Birgitte P²  Hadrup, Niels³ 

[1] National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-5460, USA;Laboratory for Molecular Pharmacology, Department of Pharmacology, The Panum Institute, University of Copenhagen, Building 18, 6, Blegdamsvej 3, DK-2200 Copenhagen, Denmark;Laboratory for Cardiovascular Pharmacology, Department of Pharmacology, The Panum Institute, University of Copenhagen, DK-2200 Copenhagen, Denmark

关键词: Dopamine receptor;    Sorting nexin 1;    Ezrin–radixin–moesin-binding phosphoprotein 50;    N-Ethylmaleimide-sensitive factor;    Protein sorting;   

DOI  :  10.1016/S0014-5793(03)01431-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The mechanisms underlying targeted sorting of endocytosed receptors for recycling to the plasma membrane or degradation in lysosomes are poorly understood. In this report, the C-terminal tails of the five dopamine receptors (D1–D5) were expressed as glutathione S-transferase (GST) fusion proteins and studied for their interaction with ezrin–radixin–moesin-binding phosphoprotein 50 (EBP50) and N-ethylmaleimide-sensitive factor (NSF), which are known to be involved in post-endocytic recycling of receptors back to the plasma membrane, and with sorting nexin 1 (SNX1), known to be involved in targeting receptors to lysosomal degradation. EBP50 did not bind any of the dopamine receptor tails. NSF bound strongly to D1 and D5 and only weakly to D2, D3 and D4. However, SNX1 clearly distinguished between D1 and D5, as only D5 bound strongly to this protein. This report shows that there are distinct interaction patterns for NSF and SNX1 to the various dopamine receptor subtypes.

【 授权许可】

Unknown