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GPR180 是高尔基体动力学域七跨膜螺旋蛋白家族的新成员。

GPR180 is a new member of the Golgi-dynamics domain seven-transmembrane helix protein family.

机构信息

Boehringer Ingelheim Pharma GmbH & Co. KG, Biberach an der Riß, Germany.

Department of Health Sciences and Technology, ETH Zürich, Zürich, Switzerland.

出版信息

Commun Biol. 2024 Nov 28;7(1):1588. doi: 10.1038/s42003-024-07260-9.

DOI:10.1038/s42003-024-07260-9
PMID:39609618
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11605061/
Abstract

GOLD domain seven-transmembrane helix (GOST) proteins form a new protein family involved in trafficking of membrane-associated cargo. They share a characteristic extracellular/luminal Golgi-dynamics (GOLD) domain, possibly responsible for ligand recognition. Based on structural homology, GPR180 is a new member of this protein family, but little is known about the cellular role of GPR180. Here we show the X-ray structure of the N-terminal domain of GPR180 (1.9 Å) and can confirm the homology to GOLD domains. Using cellular imaging we show the localization of GPR180 in intracellular vesicular structures implying its exposure to acidic pH environments. With Hydrogen/Deuterium Exchange-Mass Spectrometry (HDX-MS) we identify pH-dependent conformational changes, which can be mapped to a putative ligand binding site in the transmembrane region. The results reveal GPR180's role in intracellular vesicles and offer insights into the pH-dependent function of this conserved GOST protein.

摘要

GOST 蛋白是一类新的跨膜七螺旋束蛋白家族，它们参与膜相关货物的运输。GOST 蛋白家族成员具有特征性的胞外/腔 Golgi 动力学（GOLD）结构域，可能负责配体识别。基于结构同源性，GPR180 是该蛋白家族的一个新成员，但关于 GPR180 的细胞功能知之甚少。本文报道了 GPR180 蛋白 N 端结构域（1.9Å）的 X 射线结构，证实其与 GOLD 结构域具有同源性。利用细胞成像技术，本文显示 GPR180 定位于细胞内囊泡结构中，提示其可能暴露于酸性 pH 环境中。利用氢/氘交换质谱技术（HDX-MS），本文鉴定了 pH 依赖性构象变化，并将其映射到跨膜区的一个假定配体结合位点上。这些结果揭示了 GPR180 在细胞内囊泡中的作用，并为理解该保守 GOST 蛋白的 pH 依赖性功能提供了线索。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/5a5593b57246/42003_2024_7260_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/63494ae7fb8e/42003_2024_7260_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/cb4988cdeaa0/42003_2024_7260_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/8dd5992d0266/42003_2024_7260_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/d4333c214146/42003_2024_7260_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/ae46058bc491/42003_2024_7260_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/8ede176b9d21/42003_2024_7260_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/ca266ab7a00d/42003_2024_7260_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/5a5593b57246/42003_2024_7260_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/63494ae7fb8e/42003_2024_7260_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/cb4988cdeaa0/42003_2024_7260_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/8dd5992d0266/42003_2024_7260_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/d4333c214146/42003_2024_7260_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/ae46058bc491/42003_2024_7260_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/8ede176b9d21/42003_2024_7260_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/ca266ab7a00d/42003_2024_7260_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d04/11605061/5a5593b57246/42003_2024_7260_Fig8_HTML.jpg

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本文引用的文献

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Hepatic G Protein-Coupled Receptor 180 Deficiency Ameliorates High Fat Diet-Induced Lipid Accumulation via the Gi-PKA-SREBP Pathway.肝 G 蛋白偶联受体 180 缺乏通过 Gi-PKA-SREBP 通路改善高脂饮食诱导的脂质积累。
Nutrients. 2023 Apr 11;15(8):1838. doi: 10.3390/nu15081838.
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Lack of GPR180 ameliorates hepatic lipid depot via downregulation of mTORC1 signaling.
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Sci Rep. 2023 Feb 1;13(1):1843. doi: 10.1038/s41598-023-29135-5.
4
Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A.GOLD 结构域七跨膜螺旋蛋白家族成员 TMEM87A 的结构。
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Putting on molecular weight: Enabling cryo-EM structure determination of sub-100-kDa proteins.增加分子量：助力小于100 kDa蛋白质的冷冻电镜结构测定。
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