Proteomics

Dataset Information

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Human LHR-APEX2 time-resolved proximity proteomics

ABSTRACT: Cellular signaling by membrane G protein-coupled receptors (GPCRs) is orchestrated by a complex and diverse array of mechanisms. The dynamics of a GPCR interactome as it evolves over time and space in response to an agonist can offer a unique window on pleiotropic signaling decoding and functional selectivity at a cellular level. In this study, we employed proximity-based APEX2 proteomics to interrogate the interaction network of the GPCR for luteinizing hormone (LHR) on a sub-minute timescale. We developed an analytical approach integrating quantitative multiplexed proteomics and temporal reference profiles, providing a platform to identify the proteomic environment of APEX2-tagged LHR at the nanometer scale. LHR activity is exquisitely regulated at a spatial level, leading to identification of novel interactors including the Ras-related GTPase RAP2B that modulate both receptor signaling and post-endocytic trafficking, and providing a resource for spatiotemporal nanodomain mapping of LHR interactors across subcellular compartments.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Jack Houghton  

LAB HEAD: Edward Tate

PROVIDER: PXD053246 | Pride | 2026-03-20

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
MAS_APEX_LHRWT5B_F1.raw Raw
MAS_APEX_LHRWT5B_F2.raw Raw
MAS_APEX_LHRWT5B_F3.raw Raw
MAS_APEX_LHRWT5B_F4.raw Raw
MAS_APEX_LHRWT5B_F5.raw Raw
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Publications

Spatiotemporally resolved GPCR interactome uncovers unique mediators of receptor agonism.

Shchepinova Maria M MM   Richardson Rachel R   Houghton Jack W JW   Walker Abigail R AR   Safar Mohammed A MA   Conole Daniel D   Hanyaloglu Aylin C AC   Tate Edward W EW  

Cell chemical biology 20250501 5

Cellular signaling by membrane G protein-coupled receptors (GPCRs) is governed by a complex and diverse array of mechanisms. The dynamics of a GPCR interactome, as it evolves over time and space in response to an agonist, provide a unique perspective on pleiotropic signaling decoding and functional selectivity at the cellular level. In this study, we utilized proximity-based APEX2 proteomics to investigate the interaction network of the luteinizing hormone receptor (LHR) on a minute-to-minute ti  ...[more]

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