Introduction of ADGRB3

ADGRB3, also known as adhesion G protein-coupled receptor B3 or brain-specific angiogenesis inhibitor 3 (BAI3), is a protein encoded by the human BAI3 gene with a molecule weight of 200 kDa. As an orphan adhesion G protein-coupled receptor, BAI3 has a long N-terminus consisting of one cub domain, five BaI Thrombospondin type 1 repeats, and one hormone binding domain. It has been reported that ADGRB3 has a high affinity for C1q proteins. And, C1q added to hippocampal neurons expressing BaI3 resulted in a decrease in the number of synapses.

Function of ADGRB3 Membrane Protein

The brain angiogenesis inhibitor proteins (BAI) represent a poorly understood family of three proteins (BAI 1, 2 and 3) within the aGPCR subfamily. As a member of aGPCRs, ADGRB3 has the archetypal elements of aGPCRs with a GPCR proteolysis site (GPS) site located within the GPCR autoproteolysis inducing (GAIN) domain, a hormone-binding domain and an elongated extracellular N-terminus containing numerous glycosylation sites and adhesion repeats. Studies have shown that the expression of BAI3 is mainly limited to neural tissues of the central nervous system. In addition, BAI3 can also be found in the human heart. Recently, the BAI3 receptor has been identified in biochemical preparations of synapses both in the forebrain and in the cerebellum. What’s more, it also controls dendritic arborization growth and branching in cultured neurons. Activation of the BAI3 signaling pathway could lead to direct reorganization of the actin cytoskeleton through RhoGTPase signaling in neurons.

Fig.1 Bai3 is expressed by myoblasts and is essential for myoblast fusion. Activation of Bai3 through an as yet to be determined mechanism and its interaction with Elmo are required for myoblast fusion. (Laurin, et.al. 2014)

Application of ADGRB3 Membrane Protein in Literature

1. Sigoillot SM, et.al. The secreted protein C1QL1 and its receptor BAI3 control the synaptic connectivity of excitatory inputs converging on cerebellar Purkinje cells. Cell reports. 2015, 10(5): 820-32. PubMed ID: 25660030

This article finds that the signaling pathway formed by the secreted complement C1Q-related protein C1QL1 and BAI3 controls the stereotyped pattern of connectivity established by excitatory afferents on cerebellar Purkinje cells. And BAI3 could modulate synaptogenesis of both parallel fiber and climbing fiber afferents.

2. Hamoud N, et.al. G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates. Proceedings of the National Academy of Sciences. 2014, 111(10): 3745-50. PubMed ID: 24567399

This article suggests that BAI3 has a role in the relay of extracellular fusion signals to their intracellular effectors and it is an essential transmembrane protein for embryonic vertebrate myoblast fusion.

3. Bari MF, et.al. BAI3, CDX2 and VIL1: a panel of three antibodies to distinguish small cell from large cell neuroendocrine lung carcinomas. Histopathology. 2014, 64(4): 547-56. PubMed ID: 24266897

This article suggests that BAI3, together with CDX2 and VIL1, can be used as useful adjuncts in the diagnosis of these tumor types.

4. Bolliger MF, et.al. The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins. Proceedings of the National Academy of Sciences. 2011, 108(6): 2534-9. PubMed ID: 21262840

This article reveals that C1ql proteins are secreted signaling molecules that bind to BAI3 and act, at least in part, to regulate synapse formation and/or maintenance.

5. Antoni G, et.al. A multi-stage multi-design strategy provides strong evidence that the BAI3 locus is associated with early-onset venous thromboembolism. Journal of Thrombosis and Haemostasis. 2010, 8(12): 2671-9. PubMed ID: 20946148

This article suggests that the BAI3 locus where the rs9363864 maps can be used as a new candidate for venous thromboembolism risk.

ADGRB3 Preparation Options

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Reference

1. Laurin, et.al. (2014). Insights into the biological functions of Dock family guanine nucleotide exchange factors. Genes & development, 28(6), 533-547.

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