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Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.

Publication ,  Journal Article
He, Q-T; Xiao, P; Huang, S-M; Jia, Y-L; Zhu, Z-L; Lin, J-Y; Yang, F; Tao, X-N; Zhao, R-J; Gao, F-Y; Niu, X-G; Xiao, K-H; Wang, J; Jin, C ...
Published in: Nat Commun
April 22, 2021

Arrestins recognize different receptor phosphorylation patterns and convert this information to selective arrestin functions to expand the functional diversity of the G protein-coupled receptor (GPCR) superfamilies. However, the principles governing arrestin-phospho-receptor interactions, as well as the contribution of each single phospho-interaction to selective arrestin structural and functional states, are undefined. Here, we determined the crystal structures of arrestin2 in complex with four different phosphopeptides derived from the vasopressin receptor-2 (V2R) C-tail. A comparison of these four crystal structures with previously solved Arrestin2 structures demonstrated that a single phospho-interaction change results in measurable conformational changes at remote sites in the complex. This conformational bias introduced by specific phosphorylation patterns was further inspected by FRET and 1H NMR spectrum analysis facilitated via genetic code expansion. Moreover, an interdependent phospho-binding mechanism of phospho-receptor-arrestin interactions between different phospho-interaction sites was unexpectedly revealed. Taken together, our results provide evidence showing that phospho-interaction changes at different arrestin sites can elicit changes in affinity and structural states at remote sites, which correlate with selective arrestin functions.

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Published In

Nat Commun

DOI

EISSN

2041-1723

Publication Date

April 22, 2021

Volume

12

Issue

1

Start / End Page

2396

Location

England

Related Subject Headings

  • beta-Arrestin 1
  • Recombinant Proteins
  • Receptors, Vasopressin
  • Protein Domains
  • Protein Conformation, alpha-Helical
  • Phosphorylation
  • Phosphopeptides
  • Nuclear Magnetic Resonance, Biomolecular
  • Mutation
  • Humans
 

Citation

APA
Chicago
ICMJE
MLA
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He, Q.-T., Xiao, P., Huang, S.-M., Jia, Y.-L., Zhu, Z.-L., Lin, J.-Y., … Yu, X. (2021). Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2. Nat Commun, 12(1), 2396. https://doi.org/10.1038/s41467-021-22731-x
He, Qing-Tao, Peng Xiao, Shen-Ming Huang, Ying-Li Jia, Zhong-Liang Zhu, Jing-Yu Lin, Fan Yang, et al. “Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.Nat Commun 12, no. 1 (April 22, 2021): 2396. https://doi.org/10.1038/s41467-021-22731-x.
He Q-T, Xiao P, Huang S-M, Jia Y-L, Zhu Z-L, Lin J-Y, et al. Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2. Nat Commun. 2021 Apr 22;12(1):2396.
He, Qing-Tao, et al. “Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.Nat Commun, vol. 12, no. 1, Apr. 2021, p. 2396. Pubmed, doi:10.1038/s41467-021-22731-x.
He Q-T, Xiao P, Huang S-M, Jia Y-L, Zhu Z-L, Lin J-Y, Yang F, Tao X-N, Zhao R-J, Gao F-Y, Niu X-G, Xiao K-H, Wang J, Jin C, Sun J-P, Yu X. Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2. Nat Commun. 2021 Apr 22;12(1):2396.

Published In

Nat Commun

DOI

EISSN

2041-1723

Publication Date

April 22, 2021

Volume

12

Issue

1

Start / End Page

2396

Location

England

Related Subject Headings

  • beta-Arrestin 1
  • Recombinant Proteins
  • Receptors, Vasopressin
  • Protein Domains
  • Protein Conformation, alpha-Helical
  • Phosphorylation
  • Phosphopeptides
  • Nuclear Magnetic Resonance, Biomolecular
  • Mutation
  • Humans