Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wang, J.
Right arrow Articles by Ross, E. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wang, J.
Right arrow Articles by Ross, E. M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 270, Number 12, Issue of March 24, 1995 pp. 6488-6495
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
The Carboxyl-terminal Anchorage Domain of the Turkey -Adrenergic Receptor Is Encoded by an Alternatively Spliced Exon (*)

(Received for publication, November 28, 1994)

Jun Wang Elliott M. Ross (§)

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


ABSTRACT

The originally described cDNA of the turkey beta(1)-adrenergic receptor encodes a receptor with a carboxyl-terminal, 59-amino acid extension that was not found in several mammalian beta(1)- adrenergic receptors. This extension blocks agonist-promoted endocytosis and down-regulation of the receptor. This carboxyl-terminal domain is encoded by an exon distinct from that which encodes the body of the receptor, and the originally described cDNA results from removal of an 849-nucleotide intron. Unspliced mRNA encodes a shorter open reading frame whose translated carboxyl terminus is identical with that of the mammalian beta(1)-adrenergic receptors. There is no evidence for other introns in the coding region. Splicing of the intron to produce the nonendocytosing receptor is highest in fetal blood cells, is appreciable in adult brain and heart, and is detectable in other tissues. Thus, different tissues use alternative splicing to express beta-adrenergic receptors that either do or do not endocytose and down-regulate in response to agonist.



FOOTNOTES

*
This work was supported by a postdoctoral fellowship from Cadus Pharmaceuticals, Inc., National Institutes of Health Grant R37GM30355, and Robert A. Welch Foundation Grant I-0982. 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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank(TM)/EMBL Data Bank with accession number(s) U14958[GenBank].

§
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)
Turkeys express at least three beta-adrenergic receptor subtypes: the beta(1) subtype discussed here, a beta(2) subtype(45) , and a third subtype denoted ``4C'' (which is probably not analogous to the mammalian beta(3); (45) ). The receptor described here is beta(1) based on the predominance of its pharmacologic specificity, although it differs somewhat from mammalian beta(1)-adrenergic receptors in its affinities for some synthetic ligands(48) . Its membrane spans and short interspan loops share 81% amino acid identity with mammalian beta(1)-adrenergic receptors but only 64% identity with the mammalian beta(2) isoform. (The mammalian beta(1) isoform is similarly 64% identical with the mammalian beta(2) in these regions.) Last, the overall structure of the turkey beta(1)-adrenergic receptor gene is strikingly similar to that of the rat and monkey beta(1)-adrenergic receptor genes (this work).

(^2)
The abbreviations used are: PCR, polymerase chain reaction; RT-PCR, reverse transcriptase PCR amplification of cDNA synthesized from poly(A) RNA samples; ORF, open reading frame; bp, base pair(s).


ACKNOWLEDGEMENTS

We thank David Russell, Mark Lehrman, and Tom Wilkie for advice and discussion throughout this study, Rob Nicholas (Univ. of North Carolina) for sending us his manuscript before its publication, and Belinda Sloan-Sanchez for technical assistance. Several pilot experiments on the rat mRNA were performed by Roanna Padre. We are grateful to Carolyn Overton and the staff of Plantation Foods, Waco, TX, for assistance in obtaining tissue samples.


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


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Antimicrob. Agents Chemother.Home page
K. Young, H. Jayasuriya, J. G. Ondeyka, K. Herath, C. Zhang, S. Kodali, A. Galgoci, R. Painter, V. Brown-Driver, R. Yamamoto, et al.
Discovery of FabH/FabF Inhibitors from Natural Products
Antimicrob. Agents Chemother., February 1, 2006; 50(2): 519 - 526.
[Abstract] [Full Text] [PDF]


Home page
Toxicol SciHome page
R. J. Sommer, A. J. Hume, J. M. Ciak, J. J. VanNostrand, M. Friggens, and M. K. Walker
Early Developmental 2,3,7,8-Tetrachlorodibenzo-p-Dioxin Exposure Decreases Chick Embryo Heart Chronotropic Response to Isoproterenol but Not to Agents Affecting Signals Downstream of the Beta-Adrenergic Receptor
Toxicol. Sci., February 1, 2005; 83(2): 363 - 371.
[Abstract] [Full Text] [PDF]


Home page
Mol. Endocrinol.Home page
J. Chen and H. S. Randeva
Genomic Organization of Mouse Orexin Receptors: Characterization of Two Novel Tissue-Specific Splice Variants
Mol. Endocrinol., November 1, 2004; 18(11): 2790 - 2804.
[Abstract] [Full Text] [PDF]


Home page
Mol. Endocrinol.Home page
R. D. Catalano, T. Kyriakou, J. Chen, A. Easton, and E. W. Hillhouse
Regulation of Corticotropin-Releasing Hormone Type 2 Receptors by Multiple Promoters and Alternative Splicing: Identification of Multiple Splice Variants
Mol. Endocrinol., March 1, 2003; 17(3): 395 - 410.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
A. M. Hartmann, O. Nayler, F. W. Schwaiger, A. Obermeier, and S. Stamm
The Interaction and Colocalization of Sam68 with the Splicing-associated Factor YT521-B in Nuclear Dots Is Regulated by the Src Family Kinase p59fyn
Mol. Biol. Cell, November 1, 1999; 10(11): 3909 - 3926.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
J. Wang, A. Ducret, Y. Tu, T. Kozasa, R. Aebersold, and E. M. Ross
RGSZ1, a Gz-selective RGS Protein in Brain. STRUCTURE, MEMBRANE ASSOCIATION, REGULATION BY Galpha z PHOSPHORYLATION, AND RELATIONSHIP TO A Gz GTPase-ACTIVATING PROTEIN SUBFAMILY
J. Biol. Chem., October 2, 1998; 273(40): 26014 - 26025.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
R. M. Graham, D. M. Perez, J. Hwa, and M. T. Piascik
{alpha}1-Adrenergic Receptor Subtypes : Molecular Structure, Function, and Signaling
Circ. Res., May 1, 1996; 78(5): 737 - 749.
[Full Text]


Home page
Genome ResHome page
S Grimmond, J Lagercrantz, C Drinkwater, G Silins, S Townson, P Pollock, D Gotley, E Carson, S Rakar, M Nordenskjold, et al.
Cloning and characterization of a novel human gene related to vascular endothelial growth factor.
Genome Res., February 1, 1996; 6(2): 124 - 131.
[Abstract] [PDF]


Home page
J. Biol. Chem.Home page
E. M. Parker, P. Swigart, M. H. Nunnally, J. P. Perkins, and E. M. Ross
Carboxyl-terminal Domains in the Avian beta(1)-Adrenergic Receptor That Regulate Agonist-promoted Endocytosis
J. Biol. Chem., March 24, 1995; 270(12): 6482 - 6487.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement