Plexin-B1, PLXNB1 (3p21.31)

 https://www.ncbi.nlm.nih.gov/gene/5364

PLXNB1 

Also known as

SEP; PLXN5; PLEXIN-B1

Expression

Ubiquitous expression in skin (RPKM 13.8), kidney (RPKM 13.0) and 24 other tissues See more

Preferred Names

plexin-B1

Names

plexin 5

semaphorin receptor SEP

  XP_011532137.1  plexin-B1 isoform X1

Conserved Domains (8) summary

cd11275
Location:28 → 480

Sema_plexin_B1; The Sema domain, a protein interacting module, of Plexin B1

smart00423
Location:641 → 677

PSI; domain found in Plexins, Semaphorins and Integrins

cd01179
Location:1162 → 1249

IPT_plexin_repeat2; Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present ...

cd01180
Location:1070 → 1161

IPT_plexin_repeat1; First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present ...

cd01181
Location:1252 → 1376

IPT_plexin_repeat3; Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present ...

pfam01437
Location:481 → 527

PSI; Plexin repeat

pfam08337
Location:1562 → 2103

Plexin_cytopl; Plexin cytoplasmic RasGAP domain

cl26464
Location:681 → 839   (serine,  proline rich )

Atrophin-1; Atrophin-1 family

Atrophin-1 family

Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

Related articles in PubMed

1. Role of Plexin B1 in a Breast Cancer Cohort of Pakistani Patients and its Contribution Towards Cancer Metastasis as Indicated by an In Vitro Model. Malik MFA, et al. Anticancer Res, 2017 Aug. PMID 28739743
2. Plexin-B1 indirectly affects glioma invasiveness and angiogenesis by regulating the RhoA/αvβ3 signaling pathway and SRPK1. Chang Y, et al. Tumour Biol, 2016 Aug. PMID 26944058
3. Plexin-B1 signalling promotes androgen receptor translocation to the nucleus. Williamson M, et al. Oncogene, 2016 Feb 25. PMID 25982277 These results show that Sema4D/plexin-B1 signalling promotes the translocation of AR to the nucleus and thereby enhances AR transcriptional activity. Plexin-B1 is therefore a promising target for cancer therapy, especially in low androgen situations such as those imposed by androgen deprivation therapy.
4. Function of mutant and wild-type plexinb1 in prostate cancer cells. Damola A, et al. Prostate, 2013 Sep. PMID 23775445, Free PMC Article
5. A dual binding mode for RhoGTPases in plexin signalling. Bell CH, et al. PLoS Biol, 2011 Aug. PMID 21912513, Free PMC Article Plexins are cell surface receptors for the semaphorin family of cell guidance cues. The cytoplasmic region comprises a Ras GTPase-activating protein (GAP) domain and a RhoGTPase binding domain. Concomitant binding of extracellular semaphorin and intracellular RhoGTPase triggers GAP activity and signal transduction. The mechanism of this intricate regulation remains elusive. We present two crystal structures of the human Plexin-B1 cytoplasmic region in complex with a constitutively active RhoGTPase, Rac1. The structure of truncated Plexin-B1-Rac1 complex provides no mechanism for coupling RhoGTPase and Ras binding sites. On inclusion of the juxtamembrane helix, a trimeric structure of Plexin-B1-Rac1 complexes is stabilised by a second, novel, RhoGTPase binding site adjacent to the Ras site. Site-directed mutagenesis combined with cellular and biophysical assays demonstrate that this new binding site is essential for signalling. Our findings are consistent with a model in which extracellular and intracellular plexin clustering events combine into a single signalling output.(Figure!) (Kuva ja selitys"Kärpäsestä härkänen") https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166162/bin/pbio.1001134.g005.jpg

See all (73) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. Analysis of the interaction of Plexin-B1 and Plexin-B2 with Rnd family proteins shows lack of binding specificity.
2. The positive expression of both Sema4D and PlexinB1 was found to be an independent risk factor for a worse survival in colorectal cancer.
3. Loss of plexin B1 expression might play a pivotal role in enhancing the metastatic potential of breast cancer cells.
4. Plexin B1 expression was regulated by TMPRSS2-ERG fusion gene in prostate cancer.
5. Plexin-B1 mediates RhoA/integrin alphavbeta3 involved in the PI3K/Akt pathway and SRPK1 to influence the growth of glioma cell, angiogenesis, and motility in vitro and in vivo.
6. results show that Sema4D/plexin-B1 signaling promotes the translocation of androgen receptor to the nucleus and thereby enhances AR transcriptional activity
7. Plexin-B1 induces cutaneous squamous cell carcinoma cell proliferation, migration, and invasion by interacting with Sema4D. Plexin-B1 might serve as a useful biomarker and/or as a novel therapeutic target for cSCC.
8. Results show that decreased expression of Sema4D, plexin-B1 and -B2 was associated with local recurrence and poor prognosis of breast neoplasm.
9. Dysregulation of the vascular endothelial growth factor and semaphorin ligand-receptor families in prostate cancer metastasis
10. Blocking of CD100, plexin B1 and/or B2 in adhesion experiments have shown that both CD100 and plexins act as adhesion molecules involved in monocyte-endothelial cell binding.

  https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955613/