Journal article
Distinct in vitro interaction pattern of dopamine receptor subtypes with adaptor proteins involved in post-endocytotic receptor targeting
Laboratory for Molecular Pharmacology, Department of Pharmacology, The Panum Institute, University of Copenhagen, Building 18, 6, Blegdamsvej 3, DK-2200, Copenhagen, Denmark.1
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.
Language: | English |
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Publisher: | Wiley |
Year: | 2004 |
Pages: | 276-280 |
ISSN: | 18733468 and 00145793 |
Types: | Journal article |
DOI: | 10.1016/s0014-5793(03)01431-5 |
ORCIDs: | Schwartz, Thue W |
Animals Carrier Proteins Dopamine receptor Endocytosis Escherichia coli Ezrin–radixin–moesin-binding phosphoprotein 50 Glutathione Transferase Humans N-Ethylmaleimide-Sensitive Proteins N-Ethylmaleimide-sensitive factor Nsf protein, rat Phosphoproteins Protein Isoforms Protein sorting Rats Receptors, Dopamine Recombinant Fusion Proteins Signal Transduction Sodium-Hydrogen Exchangers Sorting nexin 1 Sulfur Radioisotopes Vesicular Transport Proteins sodium-hydrogen exchanger regulatory factor