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- W2024143047 abstract "We characterized truncations of the human vasopressin V2 receptor to determine the role of the intracellular C‐terminus (comprising about 44 amino acids) in receptor function and cell surface expression. In contrast to the wild‐type receptor, the naturally occurring mutant R337X failed to confer specific [ 3 H]AVP binding to transfected cells. In addition, no vasopressin‐sensitive adenylyl cyclase was detectable in membrane preparations of these cells. Laser scanning microscopy revealed that c‐ myc epitope‐ or green fluorescent protein‐tagged R337X mutant receptors were retained within the endoplasmic reticulum. Increasing the number of C‐terminal residues (truncations after codons 348, 354 and 356) restored G protein coupling, but revealed a length‐dependent reduction of cell surface expression. Replacement of positively charged residues within the C‐terminus by glutamine residues also decreased cell surface expression. A chimeric V2 receptor with the C‐terminus replaced by that of the β 2 ‐adrenergic receptor did not bind [ 3 H]AVP and was retained within the cell. These data suggest that residues in the N‐terminal part of the C‐terminus are necessary for correct folding and that C‐terminal residues are important for efficient cell surface expression." @default.
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- W2024143047 date "1998-03-06" @default.
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- W2024143047 title "Folding and cell surface expression of the vasopressin V2 receptor: requirement of the intracellular C‐terminus" @default.
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- W2024143047 doi "https://doi.org/10.1016/s0014-5793(98)00140-9" @default.
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