Proteomics

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MC4 crosslinking of rhodopsin and GRK1 complex

ABSTRACT: G protein-coupled receptor (GPCR) kinases (GRKs) selectively phosphorylate agonist bound GPCRs, thereby switching the signal from G protein-dependent to arrestin-dependent pathways, including receptor internalization and downregulation. There are currently no high-resolution details known about how a GRK recognizes an activated receptor, but most functional studies indicate that its unique N-terminus is key to agonist-dependent phosphorylation. Herein, we report the 7.2 Å cryo-electron microscopy (EM) single particle reconstruction of the rhodopsin-rhodopsin kinase (GRK1) complex. The structure reveals a 1:1 assembly with multiple contact points between the GRK1 kinase domain and rhodopsin, the most prominent being the insertion of the GRK1 N-terminal helix directly into the cytoplasmic cleft formed by rhodopsin in its active state. Cross-linking coupled with mass spectrometry, along with functional studies, confirmed the observed interface between the proteins and revealed regions of the complex that are dynamic.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Manolo Plasencia  

LAB HEAD: Philip C Andrews

PROVIDER: PXD019215 | Pride | 2021-07-15

REPOSITORIES: Pride

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f1-1828-HRMS2-v8chymo-rho-grk-mc4-1.zhrm Other
f1-1828-HRMS2-v8mix-rho-grk-mc4-1.pdResult Other
f1-1828-HRMS2-v8mix-rho-grk-mc4-1.raw Raw
f1-1828-HRMS2-v8tryp-rho-grk-mc4-1.zhrm Other
f2-1828-HRMS2-v8chymo-rho-grk-mc4-2.zhrm Other
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Publications

G-protein-coupled receptor (GPCR) kinases (GRKs) selectively phosphorylate activated GPCRs, thereby priming them for desensitization<sup>1</sup>. Although it is unclear how GRKs recognize these receptors<sup>2-4</sup>, a conserved region at the GRK N terminus is essential for this process<sup>5-8</sup>. Here we report a series of cryo-electron microscopy single-particle reconstructions of light-activated rhodopsin (Rho*) bound to rhodopsin kinase (GRK1), wherein the N terminus of GRK1 forms a he  ...[more]

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