Distinct in vitro interaction pattern of dopamine receptor subtypes with adaptor proteins involved in post-endocytotic receptor targeting
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Distinct in vitro interaction pattern of dopamine receptor subtypes with adaptor proteins involved in post-endocytotic receptor targeting. / Heydorn, Arne; Søndergaard, Birgitte P; Hadrup, Niels; Holst, Birgitte; Haft, Carol Renfrew; Schwartz, Thue W.
In: FEBS Letters, Vol. 556, No. 1-3, 2004, p. 276-80.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Distinct in vitro interaction pattern of dopamine receptor subtypes with adaptor proteins involved in post-endocytotic receptor targeting
AU - Heydorn, Arne
AU - Søndergaard, Birgitte P
AU - Hadrup, Niels
AU - Holst, Birgitte
AU - Haft, Carol Renfrew
AU - Schwartz, Thue W
N1 - Keywords: Animals; Carrier Proteins; Endocytosis; Escherichia coli; Glutathione Transferase; Humans; N-Ethylmaleimide-Sensitive Proteins; Phosphoproteins; Protein Isoforms; Rats; Receptors, Dopamine; Recombinant Fusion Proteins; Signal Transduction; Sodium-Hydrogen Antiporter; Sulfur Radioisotopes; Vesicular Transport Proteins
PY - 2004
Y1 - 2004
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 14706863
VL - 556
SP - 276
EP - 280
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 1-3
ER -
ID: 10536376