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Different conformational dynamics of β-arrestin1 and β-arrestin2 analyzed by hydrogen/deuterium exchange mass spectrometry.

Biochem. Biophys. Res. Commun.2015 Jan 30;457(1):50-7. Epub 2014 Dec 23
Youngjoo Yun 1 , Dong Kyun Kim 1 , Min-Duk Seo 2 , Kyeong-Man Kim 3 , Ka Young Chung 4
Youngjoo Yun 1 , Dong Kyun Kim 1 , Min-Duk Seo 2 , Kyeong-Man Kim 3 , Ka Young Chung 4

[No authors listed]

Author information
  • 1 School of Pharmacy, Sungkyunkwan University, Suwon, Republic of Korea.
  • 2 College of Pharmacy & Department of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
  • 3 College of Pharmacy, Chonnam National University, Gwang-Ju, Republic of Korea.
  • 4 School of Pharmacy, Sungkyunkwan University, Suwon, Republic of Korea. Electronic address: kychung2@skku.edu.

摘要


Arrestins have important roles in G protein-coupled receptor (GPCR) signaling including desensitization of GPCRs and G protein-independent signaling. There have been four arrestins identified: arrestin1, arrestin2 (e.g. β-arrestin1), arrestin3 (e.g. β-arrestin2), and arrestin4. β-Arrestin1 and β-arrestin2 are ubiquitously expressed and regulate a broad range of GPCRs, while arrestin1 and arrestin4 are expressed in the visual system. Although the functions of β-arrestin1 and β-arrestin2 widely overlap, β-arrestin2 has broader receptor selectivity, and a few studies have suggested that β-arrestin1 and β-arrestin2 have distinct cellular functions. Here, we compared the conformational dynamics of β-arrestin1 and β-arrestin2 by hydrogen/deuterium exchange mass spectrometry (HDX-MS). We also used the R169E mutant as a pre-activation model system. HDX-MS data revealed that β-strands II through IV were more dynamic in β-arrestin2 in the basal state, while the middle loop was more dynamic in β-arrestin1. With pre-activation, both β-arrestin1 and β-arrestin2 became more flexible, but broader regions of β-arrestin1 became flexible compared to β-arrestin2. The conformational differences between β-arrestin1 and β-arrestin2 in both the basal and pre-activated states might determine their different receptor selectivities and different cellular functions.

KEYWORDS: Conformational dynamics, Hydrogen/deuterium exchange mass spectrometry, Pre-activation, β-Arrestin