Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms

Research output: Contribution to journal › Journal article › Research › peer-review

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Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms. / Deng, Yufang; Von Moo, Ee; Inoue, Asuka; Braeuner-Osborne, Hans.

In: FEBS Letters, Vol. 597, No. 11, 2023, p. 1528-1540.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Deng, Y, Von Moo, E, Inoue, A & Braeuner-Osborne, H 2023, 'Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms', FEBS Letters, vol. 597, no. 11, pp. 1528-1540. https://doi.org/10.1002/1873-3468.14622

APA

Deng, Y., Von Moo, E., Inoue, A., & Braeuner-Osborne, H. (2023). Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms. FEBS Letters, 597(11), 1528-1540. https://doi.org/10.1002/1873-3468.14622

Vancouver

Deng Y, Von Moo E, Inoue A, Braeuner-Osborne H. Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms. FEBS Letters. 2023;597(11):1528-1540. https://doi.org/10.1002/1873-3468.14622

Author

Deng, Yufang ; Von Moo, Ee ; Inoue, Asuka ; Braeuner-Osborne, Hans. / Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms. In: FEBS Letters. 2023 ; Vol. 597, No. 11. pp. 1528-1540.

Bibtex

@article{f1b0ad831dce4da6b6451e82580ff1b6,
title = "Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms",
abstract = "GPR15 is a G protein-coupled receptor involved in immune disorders such as human immunodeficiency virus-induced enteropathy, multiple sclerosis, and colitis. Yet, the important endocytosis mechanism of GPR15 remained unclear. This study determined the participation of endocytic machinery proteins, including G alpha proteins, G protein-coupled receptor kinases (GRKs), protein kinase C, arrestins, clathrin, caveolin, and dynamin in GPR15 internalization. The results demonstrate that GPR15 internalization is moderately dependent on GRKs and clathrin, and highly dependent on caveolin and dynamin. Moreover, a bystander arrestin recruitment assay showed that GPR15 recruits arrestin-3 to the cell membrane upon agonist stimulation, although GPR15 internalizes in an arrestin-independent manner. Overall, our study provides novel insights into beta-arrestin recruitment and receptor internalization mechanisms for the recently deorphanized GPR15.",
keywords = "caveolin, clathrin, dynamin, GPR15, GRKs, internalization, COUPLED RECEPTORS, BETA-ARRESTINS, CLATHRIN, PHOSPHORYLATION, CAVEOLAE, ADAPTER, AP-2",
author = "Yufang Deng and {Von Moo}, Ee and Asuka Inoue and Hans Braeuner-Osborne",
year = "2023",
doi = "10.1002/1873-3468.14622",
language = "English",
volume = "597",
pages = "1528--1540",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "11",

}

RIS

TY - JOUR

T1 - Endocytic proteins mediating GPR15 receptor internalization provide insight into the underlying mechanisms

AU - Deng, Yufang

AU - Von Moo, Ee

AU - Inoue, Asuka

AU - Braeuner-Osborne, Hans

PY - 2023

Y1 - 2023

N2 - GPR15 is a G protein-coupled receptor involved in immune disorders such as human immunodeficiency virus-induced enteropathy, multiple sclerosis, and colitis. Yet, the important endocytosis mechanism of GPR15 remained unclear. This study determined the participation of endocytic machinery proteins, including G alpha proteins, G protein-coupled receptor kinases (GRKs), protein kinase C, arrestins, clathrin, caveolin, and dynamin in GPR15 internalization. The results demonstrate that GPR15 internalization is moderately dependent on GRKs and clathrin, and highly dependent on caveolin and dynamin. Moreover, a bystander arrestin recruitment assay showed that GPR15 recruits arrestin-3 to the cell membrane upon agonist stimulation, although GPR15 internalizes in an arrestin-independent manner. Overall, our study provides novel insights into beta-arrestin recruitment and receptor internalization mechanisms for the recently deorphanized GPR15.

AB - GPR15 is a G protein-coupled receptor involved in immune disorders such as human immunodeficiency virus-induced enteropathy, multiple sclerosis, and colitis. Yet, the important endocytosis mechanism of GPR15 remained unclear. This study determined the participation of endocytic machinery proteins, including G alpha proteins, G protein-coupled receptor kinases (GRKs), protein kinase C, arrestins, clathrin, caveolin, and dynamin in GPR15 internalization. The results demonstrate that GPR15 internalization is moderately dependent on GRKs and clathrin, and highly dependent on caveolin and dynamin. Moreover, a bystander arrestin recruitment assay showed that GPR15 recruits arrestin-3 to the cell membrane upon agonist stimulation, although GPR15 internalizes in an arrestin-independent manner. Overall, our study provides novel insights into beta-arrestin recruitment and receptor internalization mechanisms for the recently deorphanized GPR15.

KW - caveolin

KW - clathrin

KW - dynamin

KW - GPR15

KW - GRKs

KW - internalization

KW - COUPLED RECEPTORS

KW - BETA-ARRESTINS

KW - CLATHRIN

KW - PHOSPHORYLATION

KW - CAVEOLAE

KW - ADAPTER

KW - AP-2

U2 - 10.1002/1873-3468.14622

DO - 10.1002/1873-3468.14622

M3 - Journal article

C2 - 37051832

VL - 597

SP - 1528

EP - 1540

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 11

ER -

ID: 346408228