JBC

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


     

Originally published In Press as doi:10.1074/jbc.M007696200 on September 29, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1084-1088, January 12, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/2/1084    most recent
M007696200v1
Right arrow Alert me when this article is cited
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Solano, R. M.
Right arrow Articles by Waelbroeck, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Solano, R. M.
Right arrow Articles by Waelbroeck, 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?

Two Basic Residues of the h-VPAC1 Receptor Second Transmembrane Helix Are Essential for Ligand Binding and Signal Transduction*

Rosa Maria SolanoDagger , Ingrid Langer, Jason Perret, Pascale Vertongen, Maria Guillerma Juarranz§, Patrick Robberecht, and Magali Waelbroeck

From the Laboratoire de Chimie Biologique et de la Nutrition, Faculté de Médecine, Université Libre de Bruxelles, 808 route de Lennik, Building G/E, CP 611, B-1070 Brussels, Belgium

We mutated the vasoactive intestinal peptide (VIP) Asp3 residue and two VPAC1 receptor second transmembrane helix basic residues (Arg188 and Lys195). VIP had a lower affinity for R188Q, R188L, K195Q, and K195I VPAC1 receptors than for VPAC1 receptors. [Asn3] VIP and [Gln3] VIP had lower affinities than VIP for VPAC1 receptors but higher affinities for the mutant receptors; the two basic amino acids facilitated the introduction of the negatively charged aspartate inside the transmembrane domain. The resulting interaction was necessary for receptor activation. 1/[Asn3] VIP and [Gln3] VIP were partial agonists at VPAC1 receptors; 2/VIP did not fully activate the K195Q, K195I, R188Q, and R188L VPAC1 receptors; a VIP analogue ([Arg16] VIP) was more efficient than VIP at the four mutated receptors; and [Asn3] VIP and [Gln3] VIP were more efficient than VIP at the R188Q and R188L VPAC1 receptors; 3/the [Asp3] negative charge did not contribute to the recognition of the VIP1 antagonist, [AcHis1,D-Phe2,Lys15,Arg16,Leu27] VIP (1-7)/growth hormone releasing factor (8-27). This is the first demonstration that, to activate the VPAC1 receptor, the Asp3 side chain of VIP must penetrate within the transmembrane domain, in close proximity to two highly conserved basic amino acids from transmembrane 2.

* Supported by Fonds de la Recherche Scientifique Médicale Grant 3.4507.98, by an "Action de Recherche Concertée" from the Communauté Française de Belgique, by an "Interuniversity Poles of Attraction Program-Belgian State, Prime Minister's Office, Federal Office for Scientific, Technical and Cultural Affairs" and by a grant from the European Community (PACAP and VIP Euronetwork project).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of a post-doctoral fellowship from the F.R.S.M. (Belgium).

§ Recipient of a Marie Curie training grant from the European Commission. Present address: Dpt. Bioquimica y Biologia Molecular, Facultad de Medicine, Universitad de Alcalà, Ctra Madrid Barcelona, Km: 33,600, 28871 Madrid, Espana.

To whom correspondence should be addressed. Tel.: 32 2 555 62 11; Fax: 32 2 555 62 30; E-mail: mawaelbr@ulb.ac.be.

Copyright © 2001 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
 J Mol EndocrinolHome page
S. Wu, G. J Roch, L. A Cervini, J. E Rivier, and N. M Sherwood
Newly-identified receptors for peptide histidine-isoleucine and GHRH-like peptide in zebrafish help to elucidate the mammalian secretin superfamily
J. Mol. Endocrinol., November 1, 2008; 41(5): 343 - 366.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Runge, H. Thogersen, K. Madsen, J. Lau, and R. Rudolph
Crystal Structure of the Ligand-bound Glucagon-like Peptide-1 Receptor Extracellular Domain
J. Biol. Chem., April 25, 2008; 283(17): 11340 - 11347.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
E. Ceraudo, S. Murail, Y.-V. Tan, J.-J. Lacapere, J.-M. Neumann, A. Couvineau, and M. Laburthe
The Vasoactive Intestinal Peptide (VIP) {alpha}-Helix Up to C Terminus Interacts with the N-Terminal Ectodomain of the Human VIP/Pituitary Adenylate Cyclase-Activating Peptide 1 Receptor: Photoaffinity, Molecular Modeling, and Dynamics
Mol. Endocrinol., January 1, 2008; 22(1): 147 - 155.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Mies, C. Spriet, L. Heliot, and S. Sariban-Sohraby
Epithelial Na+ Channel Stimulation by n-3 Fatty Acids Requires Proximity to a Membrane-bound A-kinase-anchoring Protein Complexed with Protein Kinase A and Phosphodiesterase
J. Biol. Chem., June 22, 2007; 282(25): 18339 - 18347.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
C. Sun, D. Song, R. A. Davis-Taber, L. W. Barrett, V. E. Scott, P. L. Richardson, A. Pereda-Lopez, M. E. Uchic, L. R. Solomon, M. R. Lake, et al.
Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS
PNAS, May 8, 2007; 104(19): 7875 - 7880.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-V. Tan, A. Couvineau, S. Murail, E. Ceraudo, J.-M. Neumann, J.-J. Lacapere, and M. Laburthe
Peptide Agonist Docking in the N-terminal Ectodomain of a Class II G Protein-coupled Receptor, the VPAC1 Receptor: PHOTOAFFINITY, NMR, AND MOLECULAR MODELING
J. Biol. Chem., May 5, 2006; 281(18): 12792 - 12798.
[Abstract] [Full Text] [PDF]

Home page
 J Mol EndocrinolHome page
J C R Cardoso, D M Power, G Elgar, and M S Clark
Duplicated receptors for VIP and PACAP (VPAC1R and PAC1R) in a teleost fish, Fugu rubripes
J. Mol. Endocrinol., October 1, 2004; 33(2): 411 - 428.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-V. Tan, A. Couvineau, and M. Laburthe
Diffuse Pharmacophoric Domains of Vasoactive Intestinal Peptide (VIP) and Further Insights into the Interaction of VIP with the N-terminal Ectodomain of Human VPAC1 Receptor by Photoaffinity Labeling with [Bpa6]-VIP
J. Biol. Chem., September 10, 2004; 279(37): 38889 - 38894.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
R. C. Gensure, N. Shimizu, J. Tsang, and T. J. Gardella
Identification of a Contact Site for Residue 19 of Parathyroid Hormone (PTH) and PTH-Related Protein Analogs in Transmembrane Domain Two of the Type 1 PTH Receptor
Mol. Endocrinol., December 1, 2003; 17(12): 2647 - 2658.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-V. Tan, A. Couvineau, J. Van Rampelbergh, and M. Laburthe
Photoaffinity Labeling Demonstrates Physical Contact between Vasoactive Intestinal Peptide and the N-terminal Ectodomain of the Human VPAC1 Receptor
J. Biol. Chem., September 19, 2003; 278(38): 36531 - 36536.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Runge, C. Gram, H. Brauner-Osborne, K. Madsen, L. B. Knudsen, and B. S. Wulff
Three Distinct Epitopes on the Extracellular Face of the Glucagon Receptor Determine Specificity for the Glucagon Amino Terminus
J. Biol. Chem., July 18, 2003; 278(30): 28005 - 28010.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
I. Langer, P. Vertongen, J. Perret, M. Waelbroeck, and P. Robberecht
A Small Sequence in the Third Intracellular Loop of the VPAC1 Receptor Is Responsible for Its Efficient Coupling to the Calcium Effector
Mol. Endocrinol., May 1, 2002; 16(5): 1089 - 1096.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Lins, A. Couvineau, C. Rouyer-Fessard, P. Nicole, J.-J. Maoret, M. Benhamed, R. Brasseur, A. Thomas, and M. Laburthe
The Human VPAC1 Receptor. THREE-DIMENSIONAL MODEL AND MUTAGENESIS OF THE N-TERMINAL DOMAIN
J. Biol. Chem., March 23, 2001; 276(13): 10153 - 10160.
[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 © 2001 by the American Society for Biochemistry and Molecular Biology.