Association of small G protein ARF1 with the third intracellular loop of the M3 muscarinic receptor

2001 ◽  
Vol 29 (3) ◽  
pp. A75-A75
Author(s):  
D. N. Robertson ◽  
M. S. Johnson ◽  
P. J. Holland ◽  
R. Mitchell
Keyword(s):  
G Protein ◽  
Muscarinic Receptor ◽  
Intracellular Loop ◽  
The Third ◽  
Small G Protein ◽  
Third Intracellular Loop ◽  
M3 Muscarinic Receptor

scholarly journals Identification of Gβγ Binding Sites in the Third Intracellular Loop of the M3-muscarinic Receptor and Their Role in Receptor Regulation

2000 ◽  
Vol 275 (12) ◽  
pp. 9026-9034 ◽  
Author(s):  
Guangyu Wu ◽  
Galina S. Bogatkevich ◽  
Yurii V. Mukhin ◽  
Jeffrey L. Benovic ◽  
John D. Hildebrandt ◽  
...  
Keyword(s):  
Muscarinic Receptor ◽  
Binding Sites ◽  
Receptor Regulation ◽  
Intracellular Loop ◽  
The Third ◽  
Third Intracellular Loop ◽  
M3 Muscarinic Receptor

Presence of antibodies against the third intracellular loop of the m2 muscarinic receptor in the sera of chronic chagasic patients

1999 ◽  
Vol 13 (14) ◽  
pp. 2015-2020 ◽  
Author(s):  
Fernanda Coutinho Retondaro ◽  
Patricia C. Santos Costa ◽  
Roberto Coury Pedrosa ◽  
Eleonora Kurtenbach
Keyword(s):  
Muscarinic Receptor ◽  
Intracellular Loop ◽  
The Third ◽  
M2 Muscarinic Receptor ◽  
Third Intracellular Loop

scholarly journals A Cyclic Peptide Mimicking the Third Intracellular Loop of the V2Vasopressin Receptor Inhibits Signaling through Its Interaction with Receptor Dimer and G Protein

2004 ◽  
Vol 279 (49) ◽  
pp. 50904-50914 ◽  
Author(s):  
Sébastien Granier ◽  
Sonia Terrillon ◽  
Robert Pascal ◽  
Hélène Déméné ◽  
Michel Bouvier ◽  
...  
Keyword(s):  
G Protein ◽  
Cyclic Peptide ◽  
Intracellular Loop ◽  
The Third ◽  
Third Intracellular Loop ◽  
Receptor Dimer

scholarly journals Mutational analysis of the mouse 5-HT7 receptor: importance of the third intracellular loop for receptor-G-protein interaction

FEBS Letters ◽  
1997 ◽  
Vol 412 (2) ◽  
pp. 321-324 ◽  
Author(s):  
Louis A Obosi ◽  
René Hen ◽  
David J Beadle ◽  
Isabel Bermudez ◽  
Linda A King
Keyword(s):  
G Protein ◽  
Protein Interaction ◽  
Mutational Analysis ◽  
Intracellular Loop ◽  
The Third ◽  
Third Intracellular Loop

scholarly journals Recycling ability of the mouse and the human neurotensin type 2 receptors depends on a single tyrosine residue

2002 ◽  
Vol 115 (1) ◽  
pp. 165-173
Author(s):  
Stéphane Martin ◽  
Jean-Pierre Vincent ◽  
Jean Mazella
Keyword(s):  
G Protein ◽  
Kinase Inhibitor ◽  
Site Directed Mutagenesis ◽  
Tyrosine Residue ◽  
Receptor Recycling ◽  
Intracellular Loop ◽  
Structural Element ◽  
The Third ◽  
Third Intracellular Loop ◽  
G Protein Coupled

Receptor recycling plays a key role in the modulation of cellular responses to extracellular signals. The purpose of this work was to identify residues in G-protein coupled neurotensin receptors that are directly involved in recycling. Both the high affinity receptor-1 (NTR1) and the levocabastine-sensitive NTR2 are internalized after neurotensin binding. Here, we show that only the mouse NTR2 recycled to the plasma membrane, whereas the rat NTR1 and the human NTR2 did not. Using site-directed mutagenesis, we demonstrate that tyrosine 237 in the third intracellular loop is crucial for recycling of the mouse NTR2. We show that the mouse NTR2 is phosphorylated on tyrosine residues by NT. This phosphorylation is essential for receptor recycling since the tyrosine kinase inhibitor genistein blocks this process. The absence of recycling observed with the human NTR2 could be completely explained by the presence of a cysteine instead of a tyrosine in position 237. Indeed, substitution of this cysteine by a tyrosine gave a mutant receptor that has acquired the ability to recycle to the cell surface after neurotensin-induced internalization. This work demonstrates that a single tyrosine residue in the third intracellular loop of a G-protein-coupled receptor is responsible for receptor phosphorylation and represents an essential structural element for receptor recycling.

scholarly journals Phosphorylation and regulation of a G protein–coupled receptor by protein kinase CK2

2007 ◽  
Vol 177 (1) ◽  
pp. 127-137 ◽  
Author(s):  
Ignacio Torrecilla ◽  
Elizabeth J. Spragg ◽  
Benoit Poulin ◽  
Phillip J. McWilliams ◽  
Sharad C. Mistry ◽  
...  
Keyword(s):  
Protein Kinase ◽  
G Protein ◽  
Muscarinic Receptor ◽  
Cell Types ◽  
Intracellular Loop ◽  
Receptor Phosphorylation ◽  
Diverse Range ◽  
Jun Kinase ◽  
M3 Muscarinic Receptor ◽  
G Protein Coupled

We demonstrate a role for protein kinase casein kinase 2 (CK2) in the phosphorylation and regulation of the M3-muscarinic receptor in transfected cells and cerebellar granule neurons. On agonist occupation, specific subsets of receptor phosphoacceptor sites (which include the SASSDEED motif in the third intracellular loop) are phosphorylated by CK2. Receptor phosphorylation mediated by CK2 specifically regulates receptor coupling to the Jun-kinase pathway. Importantly, other phosphorylation-dependent receptor processes are regulated by kinases distinct from CK2. We conclude that G protein–coupled receptors (GPCRs) can be phosphorylated in an agonist-dependent fashion by protein kinases from a diverse range of kinase families, not just the GPCR kinases, and that receptor phosphorylation by a defined kinase determines a specific signalling outcome. Furthermore, we demonstrate that the M3-muscarinic receptor can be differentially phosphorylated in different cell types, indicating that phosphorylation is a flexible regulatory process where the sites that are phosphorylated, and hence the signalling outcome, are dependent on the cell type in which the receptor is expressed.

scholarly journals Down-regulation of PAR1 activity with a pHLIP-based allosteric antagonist induces cancer cell death

2015 ◽  
Vol 472 (3) ◽  
pp. 287-295 ◽  
Author(s):  
Kelly E. Burns ◽  
Damien Thévenin
Keyword(s):  
Cell Death ◽  
Cancer Cells ◽  
G Protein ◽  
Cancer Cell ◽  
Intracellular Loop ◽  
The Third ◽  
Cancer Cell Death ◽  
Third Intracellular Loop ◽  
Ph Dependent ◽  
G Protein Coupled

A pH(Low) Insertion Peptide (pHLIP)-based construct derived from the third intracellular loop (i3) of a G protein-coupled receptor (GPCR) induces a concentration- and pH-dependent cytotoxicity in cancer cells by down-regulating receptor activity. This strategy allows for a more selective intracellular delivery than current approaches.

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