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Study shows that plexin-B2 (PLXNB2) is the functional receptor for ANG (show ANG Proteins) in endothelial, cancer, neuronal, and normal hematopoietic and leukemic stem and progenitor cells.
Analysis of the interaction of Plexin-B1 (show PLXNB1 Proteins) and Plexin-B2 with Rnd family proteins shows lack of binding specificity.
plexin-B2 is a downstream target for Rnd3 (show RND3 Proteins), which contributes to its cellular function.
Results show that decreased expression of Sema4D (show SEMA4D Proteins), plexin-B1 (show PLXNB1 Proteins) and -B2 was associated with local recurrence and poor prognosis of breast neoplasm.
Two related guanine nucleotide exchange factors (GEFs), PDZ-RhoGEF (show ARHGEF11 Proteins) and leukemia-associated RhoGEF (LARG (show ARHGEF12 Proteins)), use their PDZ domains to bind class B plexins and play critical roles in signaling.
Plexin-B2 promotes glioma invasion and vascularization
Blocking of CD100 (show SEMA4D Proteins), plexin B1 (show PLXNB1 Proteins) and/or B2 in adhesion experiments have shown that both CD100 (show SEMA4D Proteins) and plexins act as adhesion molecules involved in monocyte-endothelial cell binding.
In endometrial luminal epithelium, cadherin 6 (show CDH6 Proteins), desmoglein 2 (show DSG2 Proteins) and plexin b2 were surprisingly found in the apical as well as the lateral membrane domain; their knock-down compromised epithelial integrity.
High PLEXIN B2 expression is associated with high-grade gliomas.
Plexin B2 associates directly with two members of a recently identified family of Dbl (show MCF2 Proteins) homology/pleckstrin (show PLEK Proteins) homology containing guanine nucleotide exchange factors for Rho, PDZ-RhoGEF (show ARHGEF11 Proteins), and Leukemia-associated Rho GEF (show SLC2A4RG Proteins) (LARG (show ARHGEF12 Proteins)).
Germinal center recruitment of follicular T helper cells requires Plexin B2.
Plexin-B1 (show PLXNB1 Proteins) and -B2 play redundant or compensatory roles during forebrain development to ensure proper neuronal production and neocortical expansion.
During kidney morphogenesis and repair, renal tubular epithelial cells lacking the transmembrane receptor Plexin-B2 or its semaphorin ligands fail to correctly orient the mitotic spindle
Data show that the Plexin B2 receptor interacts physically and functionally with Rnd3 (show RND3 Proteins) and stimulates RhoA (show RHOA Proteins) activity in migrating cortical neurons.
In contrast to the GAP domain mutants, Plexin-B2 transgenic mice defective in Rho guanine nucleotide exchange factor binding are viable and fertile but exhibit abnormal development of the liver vasculature
these results show that Plexin-B2 plays a role in postnatal neurogenesis and in the migration of subventricular zone-derived neuroblasts
Data an association between Plexin-B2 and Plexin-D1 (show PLXND1 Proteins) with the negative regulation of IL-12 (show IL12A Proteins)/IL-23p40 in DCs.
In vitro blocking of plexin B2 or CD100 (show SEMA4D Proteins) inhibited gamma-delta T cell activation.
Data show that Plexin-B2 functions in macrophages as a negative regulator of the GTPases Rac (show AKT1 Proteins) and Cdc42 (show CDC42 Proteins) and as a negative regulator of basal cell motility and wound healing.
deletion of Plexin B2 (Plxnb2), a semaphorin receptor that is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney, results in renal hypoplasia and occasional double ureters
Members of the B class of plexins, such as PLXNB2 are transmembrane receptors that participate in axon guidance and cell migration in response to semaphorins (Perrot et al. (2002)
, differentially expressed in brain tumors