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Article

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

Nature communications - 22 Apr 2021

He Qing-Tao, Xiao Peng, Huang Shen-Ming, Jia Ying-Li, Zhu Zhong-Liang, Lin Jing-Yu, Yang Fan, Tao Xiao-Na, Zhao Ru-Jia, Gao Feng-Yuan, Niu Xiao-Gang, Xiao Kun-Hong, Wang Jiangyun, Jin Changwen, Sun Jin-Peng, Yu Xiao

Abstract excerpt

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...

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Identifiers

PMID: 33888704
DOI: 10.1038/s41467-021-22731-x
PMCID: PMC8062632

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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