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Snapshots of the dynamic basis of NTSR1 G protein subtype promiscuity

Time-resolved cryo-electron microscopy during activation of Gα_i1βγ and Gα₁₁βγ heterotrimers bound to NTSR1 enables isolation of multiple transient complexes along the activation pathway and reveals structural motifs that stabilize these intermediates.

Alina A. Vo
Arnab Modak
Michael J. Robertson
ResearchOpen Access11 Mar 2026
Nature

Volume: 652, P: 803-811
Publisher Correction: G12/13 is activated by acute tethered agonist exposure in the adhesion GPCR ADGRL3

Signe Mathiasen
Tiago Palmisano
Jonathan A. Javitch
Amendments and Corrections17 Aug 2020
Nature Chemical Biology

Volume: 16, P: 1440
GLP-1R signaling neighborhoods associate with the susceptibility to adverse drug reactions of incretin mimetics

Agonists of the glucagon-like peptide-1 receptor are used to treat diabetes and obesity. Here, Wright et al. investigate the subcellular location of the receptor’s signaling events and uncover associations between signaling profiles and adverse drug reactions.

Shane C. Wright
Aikaterini Motso
Volker M. Lauschke
ResearchOpen Access09 Oct 2023
Nature Communications

Volume: 14, P: 1-13
The role of G protein conformation in receptor–G protein selectivity

Coupling selectivity was found to be partly lost with G proteins that bypass conformations that exist before GDP release, suggesting that selectivity is closely linked to the process of nucleotide release.

Wonjo Jang
Sumin Lu
Nevin A. Lambert
Research16 Jan 2023
Nature Chemical Biology

Volume: 19, P: 687-694
A conserved molecular switch in Class F receptors regulates receptor activation and pathway selection

Class F receptors are therapeutic targets in human disease and understanding their structural changes during receptor activation may provide important pharmacological insight. Here, the authors combine computational and experimental methods to identify a molecular switch in TM6/7 of Class F receptors that mediates receptor activation.

Shane C. Wright
Paweł Kozielewicz
Gunnar Schulte
ResearchOpen Access08 Feb 2019
Nature Communications

Volume: 10, P: 1-12
Uncoupling diffusion and binding in FRAP experiments

Nevin A Lambert
Correspondence01 Mar 2009
Nature Methods

Volume: 6, P: 183
Structure of formylpeptide receptor 2-G_i complex reveals insights into ligand recognition and signaling

Formylpeptide receptors (FPRs) are a class of chemotactic G protein-coupled receptors (GPCRs) that recognize pathogen- and host-derived formylpeptides. Here the authors report the 3.17 Å cryo-EM structure of the human FPR2-G_i signaling complex with a bound peptide agonist and in combination with computational docking and MD simulations provide mechanistic insights into formylpeptide recognition by FPRs.

Youwen Zhuang
Heng Liu
Cheng Zhang
ResearchOpen Access14 Feb 2020
Nature Communications

Volume: 11, P: 1-12
G12/13 is activated by acute tethered agonist exposure in the adhesion GPCR ADGRL3

Among the adhesion receptor class of GPCRs, which are understudied, the adhesion receptor ADGRL3 can be activated by its own tethered agonist and couples to G protein G12/13 and somewhat to Gq.

Signe Mathiasen
Tiago Palmisano
Jonathan A. Javitch
Research10 Aug 2020
Nature Chemical Biology

Volume: 16, P: 1343-1350
CODA-RET reveals functional selectivity as a result of GPCR heteromerization

Based on a BRET readout, dopamine D2 receptor agonist NPA is more potent at activating Gα_i when the D2 receptor forms a heteromer with the related D1 receptor than if it forms D2 receptor homomers, suggesting that GPCR heteromerization can result in functional selectivity.

Eneko Urizar
Hideaki Yano
Jonathan A Javitch
Research24 Jul 2011
Nature Chemical Biology

Volume: 7, P: 624-630
Pathway selectivity in Frizzleds is achieved by conserved micro-switches defining pathway-determining, active conformations

Signaling pathway selectivity downstream of GPCRs is not fully understood. Here, authors perform functional analysis of Frizzled mutants to uncover state-stabilizing residues or ‘micro-switches’ mediating selectivity towards Disheveled over G proteins.

Lukas Grätz
Maria Kowalski-Jahn
Gunnar Schulte
ResearchOpen Access29 Jul 2023
Nature Communications

Volume: 14, P: 1-17
Inactive-state preassembly of G_q-coupled receptors and G_q heterotrimers

Monitoring preassembly of the G protein–coupled receptor M3 muscarinic acetylcholine receptor M3R–G_q heterotrimers by FRAP reveals that agonist- and antagonist-insensitive preassembly of inactive-state complexes via a polybasic motif in M3R increases the sensitivity and accelerates the onset of GPCR signaling.

Kou Qin
Chunmin Dong
Nevin A Lambert
Research28 Aug 2011
Nature Chemical Biology

Volume: 7, P: 740-747
Activation of a novel α_2AAR-spinophilin-cofilin axis determines the effect of α₂ adrenergic drugs on fear memory reconsolidation

Shalini Saggu
Yunjia Chen
Qin Wang
Research10 Nov 2022
Molecular Psychiatry

Volume: 28, P: 588-600
BRET evidence that β2 adrenergic receptors do not oligomerize in cells

Tien-Hung Lan
Qiuju Liu
Nevin A. Lambert
ResearchOpen Access08 May 2015
Scientific Reports

Volume: 5, P: 1-12

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