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Volume 270, Number 12, Issue of March 24, 1995 pp. 6482-6487
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Carboxyl-terminal Domains in the Avian -Adrenergic Receptor That Regulate Agonist-promoted Endocytosis (*)

(Received for publication, November 28, 1994; and in revised form, January 10, 1995)

Eric M. Parker (§) Philip Swigart Mary H. Nunnally (¶) John P. Perkins Elliott M. Ross (**)

From the Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9041


ABSTRACT

Most G protein-coupled receptors, including the mammalian beta(2)-adrenergic receptor, are endocytosed to an intracellular, vesicular compartment upon continued exposure to agonist. The long form of the avian beta(1)-adrenergic receptor, which contains a carboxyl-terminal 59-amino acid extension, does not undergo agonist-promoted endocytosis. We constructed and expressed turkey beta(1)-adrenergic receptor cDNAs with regularly spaced carboxyl-terminal truncations and studied their agonist-promoted endocytosis. Removal of 34-86 amino acids from the carboxyl terminus of the turkey receptor allowed its efficient endocytosis, with optimal endocytosis observed upon removal of 59 residues. Removal of only 18 residues allowed some endocytosis. A receptor that lacks the entire carboxyl-terminal region (124 residues) was not endocytosed. We also constructed a chimeric hamster beta(2)-adrenergic receptor with the added 59-residue carboxyl-terminal domain of the turkey receptor. The chimera was not significantly endocytosed. These data indicate that residues 450-465 in the carboxyl-terminal region of the beta(1)-adrenergic receptor can act independently to block agonist-promoted endocytosis and that other carboxyl-terminal structures nearer to the seventh membrane span are required for endocytosis.


FOOTNOTES

*
This work was supported by National Institutes of Health Grants GM 30355 (to E. M. R.) and GM36254 (to J. P. P.) and by R. A. Welch Foundation Grant I-0982 (to E. M. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked ``advertisement'' in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§
Present address: Dept. of CNS Biology, Dept. 404, Bristol-Myers Squibb Co., 5 Research Pkwy., Wallingford, CT 06492.

Present address: Canji, Inc., San Diego, CA.

**
To whom correspondence and reprint requests should be addressed: Dept. of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75235-9041.

(^1)
The avian beta(1)-adrenergic receptor differs slightly from mammalian beta(1)-adrenergic receptors in its selectivity among some synthetic ligands(39) , but it is clearly of the beta(1) subtype according to its sequence, the organization of its gene(34) , and its overall pharmacologic specificity.

(^2)
The abbreviations used are: ICYP, (-)-iodocyanopindolol; HTCR, chimeric hamster beta(2)-adrenergic receptor to which the carboxyl-terminal region of the turkey beta(1)-adrenergic is appended.


©1995 by The American Society for Biochemistry and Molecular Biology, Inc.



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