A Dileucine Sequence and an Upstream Glutamate Residue in the Intracellular Carboxyl Terminus of the Vasopressin V2 Receptor are Essential for Cell Surface Transport in COS.M6 Cells
|Title:||A Dileucine Sequence and an Upstream Glutamate Residue in the Intracellular Carboxyl Terminus of the Vasopressin V2 Receptor are Essential for Cell Surface Transport in COS.M6 Cells|
|Authors:||Schulein, Ralf; Oksche, Alexander; Rosenthal, Walter; Hermosilla, Ricardo; Dehe, Marcel; Wiesner, Burkhard; Krause, Gerd|
|Date Published:||September 01, 1998|
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This translation by the NDI Foundation is to assist the lay reader. To provide a clear, accessible interpretation of the original article, we eliminated or simplified some technical detail and complicated scientific language. We concentrated our translation on those aspects of the article dealing directly with NDI. The NDI Foundation thanks the researchers for their work toward understanding and more effectively treating this disorder.
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Schulein, et al., examined these three residues to see if they played a role in transporting the V2R from the ER to the cell surface. They did this by creating mutated V2Rs: one missing both leucine residues and the three residues that preceded them; one that replaced the glutamate residue with glutamine; one that exchanged both leucine residues for isoleucines; one that exchanged an isoleucine for leucine 339, and one that exchanged an isoleucine for leucine 340, and three other mutants that exchanged polar threonine for the leucine as they did for the isoleucine exchange.
The authors injected each mutant V2R into a separate laboratory cell culture. Then they examined the cell cultures to see if the mutant V2Rs bound with the AVP they had introduced into the cell cultures. If they did, it meant the mutant V2Rs could get to the cell surface without the two leucine residues and the glutamate residue.
The results of their tests showed that leucine residue 339 and glutamate residue 335 are both necessary for the V2R to get from the ER to the cell surface. Leucine residue 340 has a minor but significant influence. The authors suggest that glutamate 335 and leucine 339 help fold the V2R into a shape that allows it to escape from the ER.