scholarly journals Mechanistic insights into dopaminergic and serotonergic neurotransmission – concerted interactions with helices 5 and 6 drive the functional outcome

2021 ◽  
Author(s):  
Tomasz Maciej Stepniewski ◽  
Arturo Mancini ◽  
Richard Ågren ◽  
Mariona Torrens-Fontanals ◽  
Meriem Semache ◽  
...  
Keyword(s):  
Functional Outcome ◽  
Binding Site ◽  
G Protein ◽  
Functional Response ◽  
Receptor Binding ◽  
Transmembrane Helix ◽  
Receptor Binding Site ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Serotonergic Neurotransmission

Neurotransmitter contacts within the receptor binding site differentially contribute to the overall functional response: transmembrane helix (TM) 5 contacts promote G protein coupling whereas concerted TM5–TM6 contacts enhance β-arrestin recruitment.

Subchronic haloperidol increases CB1 receptor binding and G protein coupling in discrete regions of the basal ganglia

2005 ◽  
Vol 82 (2) ◽  
pp. 264-272 ◽  
Author(s):  
Mikael Andersson ◽  
Anton Terasmaa ◽  
Kjell Fuxe ◽  
Ingrid Strömberg
Keyword(s):  
Basal Ganglia ◽  
G Protein ◽  
Receptor Binding ◽  
Cb1 Receptor ◽  
G Protein Coupling ◽  
Protein Coupling

Painful Inflammation-Induced Increase in μ-Opioid Receptor Binding and G-Protein Coupling in Primary Afferent Neurons

2003 ◽  
Vol 64 (2) ◽  
pp. 202-210 ◽  
Author(s):  
C. Zöllner ◽  
M. A. Shaqura ◽  
C. P. Bopaiah ◽  
S. Mousa ◽  
C. Stein ◽  
...  
Keyword(s):  
G Protein ◽  
Opioid Receptor ◽  
Receptor Binding ◽  
Afferent Neurons ◽  
G Protein Coupling ◽  
Primary Afferent Neurons ◽  
Primary Afferent ◽  
Protein Coupling ◽  
Μ Opioid Receptor ◽  
Opioid Receptor Binding

scholarly journals Increased opioid receptor binding and G protein coupling in the accumbens and ventral tegmental area of postnatal day 2 rats

2006 ◽  
Vol 395 (3) ◽  
pp. 244-248 ◽  
Author(s):  
Yanning Hou ◽  
Mariana M. Belcheva ◽  
Amy L. Clark ◽  
Daniel S. Zahm ◽  
Carmine J. Coscia
Keyword(s):  
Ventral Tegmental Area ◽  
G Protein ◽  
Opioid Receptor ◽  
Receptor Binding ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Ventral Tegmental ◽  
Opioid Receptor Binding

scholarly journals Position of Transmembrane Helix 6 Determines Receptor G Protein Coupling Specificity

2014 ◽  
Vol 136 (32) ◽  
pp. 11244-11247 ◽  
Author(s):  
Alexander S. Rose ◽  
Matthias Elgeti ◽  
Ulrich Zachariae ◽  
Helmut Grubmüller ◽  
Klaus Peter Hofmann ◽  
...  
Keyword(s):  
G Protein ◽  
Transmembrane Helix ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Coupling Specificity

scholarly journals Evidence of a Potential Receptor-Binding Site on the Nipah Virus G Protein (NiV-G): Identification of Globular Head Residues with a Role in Fusion Promotion and Their Localization on an NiV-G Structural Model

2006 ◽  
Vol 80 (15) ◽  
pp. 7546-7554 ◽  
Author(s):  
Vanessa Guillaume ◽  
Hamide Aslan ◽  
Michelle Ainouze ◽  
Mathilde Guerbois ◽  
T. Fabian Wild ◽  
...  
Keyword(s):  
Binding Site ◽  
G Protein ◽  
Receptor Binding ◽  
Measles Virus ◽  
Structural Model ◽  
Nipah Virus ◽  
Hendra Virus ◽  
Receptor Binding Site ◽  
Globular Head

ABSTRACT As a preliminary to the localization of the receptor-binding site(s) on the Nipah virus (NiV) glycoprotein (NiV-G), we have undertaken the identification of NiV-G residues that play a role in fusion promotion. To achieve this, we have used two strategies. First, as NiV and Hendra virus (HeV) share a common receptor and their cellular tropism is similar, we hypothesized that residues functioning in receptor attachment could be conserved between their respective G proteins. Our initial strategy was to target charged residues (which can be expected to be at the surface of the protein) conserved between the NiV-G and HeV-G globular heads. Second, we generated NiV variants that escaped neutralization by anti-NiV-G monoclonal antibodies (MAbs) that neutralize NiV both in vitro and in vivo, likely by blocking receptor attachment. The sequencing of such “escape mutants” identified NiV-G residues present in the epitopes to which the neutralizing MAbs are directed. Residues identified via these two strategies whose mutation had an effect on fusion promotion were localized on a new structural model for the NiV-G protein. Our results suggest that seven NiV-G residues, including one (E533) that was identified using both strategies, form a contiguous site on the top of the globular head that is implicated in ephrinB2 binding. This site commences near the shallow depression in the center of the top surface of the globular head and extends to the rim of the barrel-like structure on the top loops of β-sheet 5. The topology of this site is strikingly similar to that proposed to form the SLAM receptor site on another paramyxovirus attachment protein, that of the measles virus hemagglutinin.

Defect of receptor-G protein coupling in human gallbladder with cholesterol stones

2000 ◽  
Vol 278 (2) ◽  
pp. G251-G258 ◽  
Author(s):  
Zuo-Liang Xiao ◽  
Qian Chen ◽  
Joseph Amaral ◽  
Piero Biancani ◽  
Jose Behar
Keyword(s):  
G Protein ◽  
Receptor Binding ◽  
Binding Capacity ◽  
G Protein Coupling ◽  
Human Gallbladder ◽  
Protein Coupling ◽  
Cck Receptors ◽  
Protein Quantitation ◽  
Gtpγs Binding ◽  
Contraction And Relaxation

Human gallbladders with cholesterol stones (ChS) exhibit an impaired muscle contraction and relaxation and a lower CCK receptor-binding capacity compared with those with pigment stones (PS). This study was designed to determine whether there is an abnormal receptor-G protein coupling in human gallbladders with ChS using35S-labeled guanosine 5′- O-(3-thiotriphosphate) ([35S]GTPγS) binding,125I-labeled CCK-8 autoradiography, immunoblotting, and G protein quantitation. CCK and vasoactive intestinal peptide caused significant increases in [35S]GTPγS binding to Gαi-3 and Gsα, respectively. The binding was lower in ChS than in PS ( P < 0.01). The reduced [35S]GTPγS binding in ChS was normalized after the muscles were treated with cholesterol-free liposomes ( P < 0.01). Autoradiography and immunoblots showed a decreased optical density (OD) for CCK receptors, an even lower OD value for receptor-G protein coupling, and a higher OD for uncoupled receptors or Gαi-3 protein in ChS compared with PS ( P < 0.001). G protein quantitation also showed that there were no significant differences in the Gαi-3 and Gsα content in ChS and PS. We conclude that, in addition to an impaired CCK receptor-binding capacity, there is a defect in receptor-G protein coupling in muscle cells from gallbladder with ChS. These changes may be normalized after removal of excess cholesterol from the plasma membrane.

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