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BAI3


Official Full Name
adhesion G protein-coupled receptor B3
Organism
Homo sapiens
Gene ID
577
Background
This p53-target gene encodes a brain-specific angiogenesis inhibitor, a seven-span transmembrane protein, and is thought to be a member of the secretin receptor family. Brain-specific angiogenesis proteins BAI2 and BAI3 are similar to BAI1 in structure, have similar tissue specificities, and may also play a role in angiogenesis. [provided by RefSeq, Jul 2008]
Synonyms
ADGRB3; BAI3

Cat.No. Product Name Price
SHG039319 shRNA set against Human ADAM9(NM_003816.2) Inquiry
SHG039373 shRNA set against Mouse Adam9(NM_007404.2) Inquiry
SHH231702 shRNA set against Human Adam9 (NM_003816.2) Inquiry
SHH231706 shRNA set against Mouse Adam9 (NM_007404.2) Inquiry
SHH231710 shRNA set against Rat Adam9 (NM_001014772.1) Inquiry
SHH244738 shRNA set against Human BAI3 (NM_001704.2) Inquiry
SHH244742 shRNA set against Mouse BAI3 (NM_175642.4) Inquiry
SHH244746 shRNA set against Rat BAI3 (NM_001106898.1) Inquiry
SHW001989 shRNA set against Chicken ADAM9 (NM_001031396) Inquiry
SHW007272 shRNA set against Danio rerio ADAM9 (NM_001004678) Inquiry
Cat.No. Product Name Price
CDCS410389 Human BAI3 ORF Clone (BC111720) Inquiry
MiUTR1M-01192 ADAM9 miRNA 3'UTR clone Inquiry
MiUTR1H-00797 BAI3 miRNA 3'UTR clone Inquiry
MiUTR1H-00165 ADAM9 miRNA 3'UTR clone Inquiry
CDFR006623 Rat Bai3 cDNA Clone(NM_001106898.1) Inquiry
CDFR003385 Rat Adam9 cDNA Clone(NM_001014772.1) Inquiry
CDFH000323 Human ADAM9 cDNA Clone(NM_003816.2) Inquiry
CDFH000322 Human ADAM9 cDNA Clone(NM_003816.2) Inquiry
MiUTR1R-00122 ADAM9 miRNA 3'UTR clone Inquiry
SKO1004 ADAM9 Validated sgRNA vector Inquiry
CDCR286214 Human ADAM9 ORF Clone(NM_003816.2) Inquiry
CDCS411483 Human ADAM9 ORF Clone (BC126406) Inquiry
CDCR370395 Rat Adam9 ORF Clone(NM_001014772.1) Inquiry
CDCR033072 Mouse Bai3 ORF clone (NM_175642.4) Inquiry
CDCL182587 Mouse ADAM9 ORF clone(NM_007404.2) Inquiry
CDCB195448 Rabbit ADAM9 ORF clone (XM_002720772.2) Inquiry
CDCB188886 Rabbit BAI3 ORF clone (XM_002714524.2) Inquiry
CDCB168747 Danio rerio ADAM9 ORF Clone (NM_001004678) Inquiry
CDCR373675 Rat Bai3 ORF Clone(NM_001106898.1) Inquiry
CDCB163464 Chicken ADAM9 ORF Clone (NM_001031396) Inquiry

Detailed Information

The adhesion GPCR BAI3 is an orphan receptor that has a long N-terminus consisting of one cub domain, five Bal thrombospondin type 1 repeats, and one hormone binding domain.

BAI3 regulate Rac pathway

Muscle fibers are formed after fusion of muscle cells, but cell surface receptors that regulate this process are not known in vertebrates. Genetic screening of Drosophila reveals cytoskeletal regulators, including myoblast city (mbc, ortholog of Dock1) and Rac, which specifically control the myoblast fusion step. Dock1 and Rac1 mutated in mice were generated to address whether this pathway plays a universal role in myoblast fusion. Mutants die at birth and are characterized by a strong block of fusion in primary myoblasts in vivo and in vitro. Similarly, muscle-specific inactivation of Rac1 severely impairs myoblast fusion. Looking for regulators of myoblast fusion, Noumeira et al. identified the G-protein coupled receptor brain-specific angiogenesis inhibitor (BAI3) as a cell surface protein that interacts with engulfment and cell motility (ELMO). In cultured cells, loss of BAI3 or ELMO1/2 function severely impairs myoblast fusion without affecting differentiation and cannot be rescued by re-expressing BAI3 mutants lacking ELMO binding. The related BAI protein family member ember BAI1 is functionally different from BAI3 because it does not rescue myoblast fusion defects caused by loss of BAI3 function. Finally, embryonic muscle precursor expression that does not bind to ELMO's BAI3 mutant is sufficient to block myoblast fusion in vivo.

Collectively, the BAI3 plays an important role in extracellular fusion signaling to intracellular effectors, identifying it as an essential transmembrane protein for embryonic vertebrate myoblast fusion.

Fig. 1. BAI3 is expressed by myoblasts and is essential for myoblast fusion. (Laurin M et al. Genes & Development. 2014.).

Regulation of dendritic morphogenesis involves the integration of extracellular signals and intrinsic molecular programs to control the growth and branching of the actin cytoskeleton. The BAI receptors are new regulators of this process that can sense extracellular signals and Intracellular signal by interaction with effectors such as ELMO1. The BAI3 receptor was also found to localize to actin-rich cell processes, such as filopodia and lamelipodia in HEK-293H cells, as well as dendrites. V Lanoue et al. has shown that overexpression of the BAI3 receptor inhibits cell spreading through its cytoplasmic tail, partially through ELMO1, indicating that BAI3 signaling can indeed regulate dendritic morphogenesis through Rac regulation. BAI3’s interaction with ELMO1 constitutes a direct pathway linking extracellular cues and intracellular modification of the actin cytoskeleton during neuronal development.

BAI3 is a high-affinity receptor for C1q-like proteins

The C1q-like (C1q1) protein is a small secreted protein belonging to a large family of proteins containing a globular complementary 1Q (gC1q) domain that binds to form a homo-trimer or a hetero-trimer. The C1q1 and BAI3 proteins are expressed almost exclusively in the brain in adult animals and appear to be enriched in neurons. Strikingly, the addition of the recombinant gC1q domains of C1ql proteins to the medium of cultured hippocampal neurons caused significant decreases in synapse density without affecting other measured morphological parameters. Bolliger et al. revealed that the thrombospondin repeats of BAI3 were both necessary and sufficient to bind to C1ql3, and the BAI3 fragment binding to C1ql3 blocked the effect of C1ql3 on synapse density.

References:

  1. Laurin M, Côté J-F. Insights into the biological functions of Dock family guanine nucleotide exchange factors. Genes & Development. 2014;28(6):533-547.
  2. Tesmer JJG. A GAIN in understanding autoproteolytic G protein-coupled receptors and polycystic kidney disease proteins. The EMBO Journal. 2012;31(6):1334-1335. doi:10.1038/emboj.2012.51.
  3. Hamoud N, Tran V, Croteau L-P, Kania A, Côté J-F. G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates. Proceedings of the National Academy of Sciences of the United States of America. 2014;111(10):3745-3750.
  4. Duman JG, Tu Y-K, Tolias KF. Emerging Roles of BAI Adhesion-GPCRs in Synapse Development and Plasticity. Neural Plasticity. 2016; 2016:8301737.
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