HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kobilka, B. K. Search for Related Content PubMed PubMed Citation Articles by Kobilka, B. K. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 13, 7610-7618, 05, 1990

The role of cytosolic and membrane factors in processing of the human beta-2 adrenergic receptor following translocation and glycosylation in a cell-free system

BK Kobilka
Department of Medicine (Cardiology), Duke University Medical Center, Durham, North Carolina 27710.

The beta-2 adrenergic receptor has been proposed to have seven membrane- spanning domains. Expression of functional beta-2 adrenergic receptor was achieved in a heterologous cell-free system composed of rabbit reticulocyte lysate and microsomal membranes from Xenopus laevis oocytes. The functional state of the receptor protein can be determined by ligand-binding assays and by the ability of ligands to alter the susceptibility of the receptor to proteinase K digestion. The process by which functional receptor is made was studied. The receptor protein remains nonfunctional immediately following translocation and glycosylation, and additional processing steps are needed before the receptor is able to interact with ligands. These processing steps require intact microsomal membranes as well as several cytosolic factors including ATP and one or more high molecular mass (greater than 30 kDa) factors but do not require receptor glycosylation and are not inhibited by nonhydrolyzable GTP analogues.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				T. T. Leskela, P. M. H. Markkanen, E. M. Pietila, J. T. Tuusa, and U. E. Petaja-Repo Opioid Receptor Pharmacological Chaperones Act by Binding and Stabilizing Newly Synthesized Receptors in the Endoplasmic Reticulum J. Biol. Chem., August 10, 2007; 282(32): 23171 - 23183. [Abstract] [Full Text] [PDF]

				G. Swaminath, Y. Xiang, T. W. Lee, J. Steenhuis, C. Parnot, and B. K. Kobilka Sequential Binding of Agonists to the {beta}2 Adrenoceptor: KINETIC EVIDENCE FOR INTERMEDIATE CONFORMATIONAL STATES J. Biol. Chem., January 2, 2004; 279(1): 686 - 691. [Abstract] [Full Text] [PDF]

				A. A. Osman, M. Saito, C. Makepeace, M. A. Permutt, P. Schlesinger, and M. Mueckler Wolframin Expression Induces Novel Ion Channel Activity in Endoplasmic Reticulum Membranes and Increases Intracellular Calcium J. Biol. Chem., December 26, 2003; 278(52): 52755 - 52762. [Abstract] [Full Text] [PDF]

				I. D. Alves, Z. Salamon, E. Varga, H. I. Yamamura, G. Tollin, and V. J. Hruby Direct Observation of G-protein Binding to the Human {delta}-Opioid Receptor Using Plasmon-Waveguide Resonance Spectroscopy J. Biol. Chem., December 5, 2003; 278(49): 48890 - 48897. [Abstract] [Full Text] [PDF]

				Y. Lu, I. R. Turnbull, A. Bragin, K. Carveth, A.S. Verkman, and W. R. Skach Reorientation of Aquaporin-1 Topology during Maturation in the Endoplasmic Reticulum Mol. Biol. Cell, September 1, 2000; 11(9): 2973 - 2985. [Abstract] [Full Text]

				R. Brys, K. Josson, M. P. Castelli, M. Jurzak, P. Lijnen, W. Gommeren, and J. E. Leysen Reconstitution of the Human 5-HT1D Receptor-G-Protein Coupling: Evidence for Constitutive Activity and Multiple Receptor Conformations Mol. Pharmacol., June 1, 2000; 57(6): 1132 - 1141. [Abstract] [Full Text]

				U. Gether and B. K. Kobilka G Protein-coupled Receptors. II. MECHANISM OF AGONIST ACTIVATION J. Biol. Chem., July 17, 1998; 273(29): 17979 - 17982. [Full Text] [PDF]

				U. Gether, S. Lin, and B. K. Kobilka Fluorescent Labeling of Purified beta(2) Adrenergic Receptor J. Biol. Chem., November 24, 1995; 270(47): 28268 - 28275. [Abstract] [Full Text] [PDF]

				P. Ghanouni, Z. Gryczynski, J. J. Steenhuis, T. W. Lee, D. L. Farrens, J. R. Lakowicz, and B. K. Kobilka Functionally Different Agonists Induce Distinct Conformations in the G Protein Coupling Domain of the beta 2 Adrenergic Receptor J. Biol. Chem., June 29, 2001; 276(27): 24433 - 24436. [Abstract] [Full Text] [PDF]

				J.-G. Liu, M. B. Ruckle, and P. L. Prather Constitutively Active {micro}-Opioid Receptors Inhibit Adenylyl Cyclase Activity in Intact Cells and Activate G-proteins Differently than the Agonist [D-Ala2,N-MePhe4,Gly-ol5]Enkephalin J. Biol. Chem., October 5, 2001; 276(41): 37779 - 37786. [Abstract] [Full Text] [PDF]