Proteomics

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Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers

ABSTRACT: -arrestins (arr1 and arr2) are ubiquitous regulators of G protein-coupled receptor (GPCR) signalling. Available data suggest that -arrestins dock to different receptors in different ways. However, the structural characterization of arrestin-GPCR complexes is challenging and alternative approaches to study arrestin-GPCR complexes are needed. Here, starting from the finger loop as a major site for the interaction of arrestins with GPCRs, we genetically incorporate non-canonical amino acids for photo- and chemical crosslinking into arr1 and arr2 and explore binding topologies to GPCRs forming either stable or transient complexes with arrestin: the vasopressin receptor 2 (rhodopsin-like), the corticotropin releasing factor receptor 1 and the parathyroid hormone receptor 1 (both secretin-like). We show that each receptor leaves a unique footprint on arrestin, whereas the two -arrestins yield quite similar crosslinking patterns. Furthermore, we show that the method allows defining the orientation of arrestin respect to the GPCR. Finally, we provide direct evidence for the formation of arrestin oligomers in the cell.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Christian Ihling  

LAB HEAD: Andrea Sinz

PROVIDER: PXD020418 | Pride | 2020-09-21

REPOSITORIES: Pride

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Dataset's files

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Action DRS
Arr_TG2.msf Msf
Arr_TG2.raw Raw
Arr_Tryp2.msf Msf
Arr_Tryp2.raw Raw
Arr_both.mzML Mzml
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Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers.

Böttke Thore T   Ernicke Stefan S   Serfling Robert R   Ihling Christian C   Burda Edyta E   Gurevich Vsevolod V VV   Sinz Andrea A   Coin Irene I  

EMBO reports 20200914 11

β-arrestins (βarr1 and βarr2) are ubiquitous regulators of G protein-coupled receptor (GPCR) signaling. Available data suggest that β-arrestins dock to different receptors in different ways. However, the structural characterization of GPCR-arrestin complexes is challenging and alternative approaches to study GPCR-arrestin complexes are needed. Here, starting from the finger loop as a major site for the interaction of arrestins with GPCRs, we genetically incorporate non-canonical amino acids for  ...[more]

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