Dataset Information

TurboID-catalyzed proximity biotin labeling of S1PR1-WT/-TM4

ABSTRACT: Proximal proteins to S1PR1-WT and S1PR1-TM4 (a swap mutant of the transmembrane domain 4 with that of S1PR3) were obtained in human umbilical vein endothelial cells by a TurboID-catalyzed proximity biotin labeling technique.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hideru Obinata

PROVIDER: PXD039461 | JPOST Repository | Sun May 21 00:00:00 BST 2023

REPOSITORIES: jPOST

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	W1_200210_Obinata_14.mgf	Mgf
	W1_200210_Obinata_14.mzid	Mzid
	W1_200210_Obinata_14.wiff	Wiff
	W1_210616_Obinata_6.mgf	Mgf
	W1_210616_Obinata_6.mzid	Mzid

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Publications

Actin-binding protein filamin B regulates the cell-surface retention of endothelial sphingosine 1-phosphate receptor 1.

Zhao Xian X Kiyozuka Keisuke K Konishi Akimitsu A Kawabata-Iwakawa Reika R Minamishima Yoji Andrew YA Obinata Hideru H

The Journal of biological chemistry 20230521 7

Sphingosine 1-phosphate receptor 1 (S1PR1) is a G protein-coupled receptor essential for vascular development and postnatal vascular homeostasis. When exposed to sphingosine 1-phosphate (S1P) in the blood of ∼1 μM, S1PR1 in endothelial cells retains cell-surface localization, while lymphocyte S1PR1 shows almost complete internalization, suggesting the cell-surface retention of S1PR1 is endothelial cell specific. To identify regulating factors that function to retain S1PR1 on the endothelial cell ...[more]

PMID: 37220855

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Project description:Classical methods of investigating protein-protein interactions (PPIs) are generally performed in non-living systems, yet in recent years new technologies utilizing proximity labeling (PL) have given researchers the tools to explore proximal PPIs in living systems. PL has distinct advantages over traditional protein interactome studies, such as the ability to identify weak and transient interactions in vitro and in vivo. Most PL studies are performed on targets within or on the cell membrane. We have adapted the original PL method to investigate PPIs within the extracellular compartment, using both BioID2 and TurboID, that we term extracellular PL (ePL). To demonstrate the utility of this modified technique, we investigate the interactome of the widely expressed matrisome protein Tissue inhibitors of metalloproteinases 2 (TIMP2). Tissue inhibitors of metalloproteinases (TIMPs) are a family of multi-functional proteins that were initially defined by their ability to inhibit the enzymatic activity of metalloproteinases (MPs), the major mediators of extracellular matrix (ECM) breakdown and turnover. TIMP2 exhibits a broad expression profile and is often abundant in both normal and diseased tissues. Understanding the functional transformation of matrisome regulators, like TIMP2, during the evolution of tissue microenvironments associated with disease progression is essential for the development of ECM targeted therapeutics. Using carboxyl- and amino-terminal fusion proteins of TIMP2 with BioID2 and TurboID, we describe the TIMP2 proximal interactome. We also illustrate how the TIMP2 interactome changes in the presence of different stimuli, in different cell types, in unique culture conditions (2D vs 3D), and with different reaction kinetics (BioID2 vs. TurboID); demonstrating the power of this technique versus classical PPI methods. We propose that the screening of matrisome targets in disease models using ePL will reveal new therapeutic targets for further comprehensive studies.