Abstract
We recently demonstrated that the mouse EP3beta receptor and its carboxyl-terminal tail-truncated receptor showed agonist-dependent and full constitutive Gi activities, respectively (Hasegawa, H., Negishi, M. and Ichikawa, A. (1996) J. Biol. Chem. 271, 1857-1860). To assess the role of the carboxyl-terminal tail in the EP3beta receptor Gi coupling, we constructed a series of mutant receptors with progressively truncated carboxyl-termini. The truncated receptors displayed constitutive Gi activities, the degree of constitutive activity basically correlating with the inverse of the length of the carboxyl-terminal tail, but the sequence between Leu340 and Val347 was mainly contributed to the constitutive activity. Thus, the carboxyl-terminal tail plays an important role in the constraint of the EP3 receptor in its inactive conformation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenylyl Cyclases / metabolism*
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Alprostadil / analogs & derivatives
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Alprostadil / pharmacology
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Animals
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CHO Cells
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Cricetinae
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Cyclic AMP / metabolism
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GTP-Binding Proteins / metabolism*
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Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
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Kinetics
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Leucine
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Macromolecular Substances
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Mice
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Models, Structural
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Mutagenesis, Site-Directed
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Polymerase Chain Reaction
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Prostaglandins E, Synthetic / pharmacology
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Protein Conformation
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Receptors, Prostaglandin E / chemistry*
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Receptors, Prostaglandin E / metabolism
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Receptors, Prostaglandin E / physiology*
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Receptors, Prostaglandin E, EP3 Subtype
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Deletion
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Transfection
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Valine
Substances
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Macromolecular Substances
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Prostaglandins E, Synthetic
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Ptger3 protein, mouse
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Receptors, Prostaglandin E
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Receptors, Prostaglandin E, EP3 Subtype
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Recombinant Proteins
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Guanosine 5'-O-(3-Thiotriphosphate)
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11-deoxy-16-phenoxy-17,18,19,20-tetranorprostaglandin E1
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Cyclic AMP
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GTP-Binding Proteins
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Adenylyl Cyclases
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Alprostadil
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Leucine
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Valine