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Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins.
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The role of an ALK2 mutation (R258S) in IRIDA (show TMPRSS6 Proteins) development in a patient also bearing compound heterozygous mutations in TMPRSS6 (show TMPRSS6 Proteins) was demonstrated by reconstructing in vitro the proband's genotype, expressing mutants TMPRSS6 (show TMPRSS6 Proteins) and ACVR1 in the presence of hemojuvelin (show HFE2 Proteins) and assessing hepcidin (show HAMP Proteins) activation. ALK2(R258S) maintained high hepcidin (show HAMP Proteins) expression in the presence of MT2 (show MT2 Proteins)(I212T).
activation of AMPK (show PRKAA1 Proteins) upregulated Smad6 (show SMAD6 Proteins) and Smurf1 (show SMURF1 Proteins) and thereby enhanced their interactions, resulting in its proteosome-dependent degradation of ALK2.
the Fibrodysplasia Ossificans Progressiva mutation ACVR1(R206H) is more sensitive to a number of natural ligands.
both bone morphogenetic protein 2 (BMP2 (show BMP2 Proteins)) and BMP6 (show BMP6 Proteins) are proangiogenic in vitro and ex vivo and that the BMP type I receptors, activin receptor-like kinase 3 (ALK3 (show BMPR1A Proteins)) and ALK2, play crucial and distinct roles in this process.
Fibrodysplasia ossificans progressiva (FOP) syndrome is caused by mutation of the gene ACVR1. Developed is a simplified one-step procedure by simultaneously introducing reprogramming and gene-editing components into human fibroblasts derived from patient with FOP. The one-step-mediated ALK2 gene-corrected induced pluripotent stem cells restored global gene expression pattern.
The ACVR1 R206H mutation may not directly increase the formation of mature chondrogenic or osteogenic cells.
Authors demonstrated that the BMP type I receptor ALK-2 (encoded by the ACVR1 gene) has crucial roles in apoptosis induction of patient-derived glioma-initiating cells (GICs), TGS (show LIN9 Proteins)-01 and TGS (show LIN9 Proteins)-04.
Data suggest BMP9/GDF2 (show GDF2 Proteins) and BMP10 (show BMP10 Proteins) synergize with TNFA (show TNF Proteins) to increase monocyte recruitment to vascular endothelial cells; process appears to be mediated mainly via ALK2/ACVR1 (which exhibits protein kinase (show CDK7 Proteins) activity). These studies used in vitro flow monocyte adhesion assay. (BMP9 (show GDF2 Proteins) = growth differentiation factor 2 (show GDF2 Proteins); BMP10 (show BMP10 Proteins) = bone morphogenetic protein 10 (show BMP10 Proteins); TNFA (show TNF Proteins) = tumor necrosis factor alpha (show TNF Proteins); ALK2/ACVR1 = activin A receptor type 1)
The effects of ACVR1/ALK2 mutations causing fibrodysplasia ossificans progressiva are extended to the central nervous system. Brainstem hamartomatous lesions and dysmorphisms, variably associated with dentate nucleus and basal ganglia signal abnormalities and/or calcifications, may represent useful disease hallmarks.
Low ALK2 expression is associated with invasiveness of breast cancer.
NODAL/Activin signaling induces dramatic chromatin landscape changes, and a dynamic transcriptional network regulated by SMAD2 (show SMAD2 Proteins), acting via multiple mechanisms.
Acute tacrolimus treatment transiently increases hepcidin (show HAMP Proteins) in wild-type mice. FKBP12 (show FKBP1A Proteins) preferentially targets the BMP receptor (show BMPR1A Proteins) ALK2. ALK2 mutants defective in binding FKBP12 (show FKBP1A Proteins) increase hepcidin (show HAMP Proteins) expression in a ligand-independent manner, through BMP-SMAD (show SMAD1 Proteins) signaling.
The authors demonstrated that ubiquitin-specific protease (USP) 4 (show USP4 Proteins) strongly induces activin/BMP signaling by removing the inhibitory monoubiquitination from SMAD4 (show SMAD4 Proteins).
Enhanced SMAD (show SMAD1 Proteins)-dependent BMP signaling through constitutively active ACVR1 in palatal epithelium causes submucous cleft palate in mice, via medial-edge-epithelium persistence presumably due to the up regulation of DeltaNp63 andresultingreductionofcaspase-3 activation. 2.
BMP signaling mediated by coordination of ALK2/ACVR1, ALK3/BMPR1A (show BMPR1A Proteins), and BMPR2 (show BMPR2 Proteins) is an essential proangiogenic cue for retinal vessels.
This study showed that Gja1 (show GJA1 Proteins) may act downstream of cAMP-PKA signal to mediate the effects of Acvr1 on the differentiation of uterine stromal cells through targeting Hand2 (show HAND2 Proteins).
Results showed activin-C and follistatin are differentially expressed during prostate development and suggested that the antagonistic property of follistatin is secondary to the action of activin-C. Study provides evidence to support a role of activin-C in prostate development and provides new insights in the spatiotemporal localization of activins and their antagonists during mouse prostate development.
BMPR1B plays distinct roles from BMPR1A and ACVR1 in maintaining bone mass and transducing BMP signaling
Suggest that BMP signaling upregulates the calcineurin/nuclear factor of activated T cell (show NFATC3 Proteins) pathway via BMP type I receptor ALK2, contributing to cardiac hypertrophy and fibrosis.
results suggest that ACVR1(R206H) causes FOP (show CHTOP Proteins) by gaining responsiveness to the normally antagonistic ligand activin A (show INHBA Proteins), demonstrating that this ligand is necessary and sufficient for driving HO in a genetically accurate model of FOP (show CHTOP Proteins)
Data suggest that ACVR1 mRNA and protein are present in granulosa cells of ovarian follicles at mid-estrous and pre-ovulatory stages; ACVR1 mRNA and protein are also present in exosomes isolated from mid-estrous and preovulatory follicles.
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I ( I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling\; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type I receptor which signals a particular transcriptional response in concert with activin type II receptors. Mutations in this gene are associated with fibrodysplasia ossificans progressive.
TGF-B superfamily receptor type I
, activin A receptor, type II-like kinase 2
, activin receptor type I
, activin receptor type-1
, activin receptor-like kinase 2
, hydroxyalkyl-protein kinase
, serine/threonine-protein kinase receptor R1
, activin A receptor, type 1
, activin type I receptor
, type I TGF B receptor
, activin A receptor, type I
, activin receptor type IA
, activin A receptor type 1 S homeolog
, activin A receptor type I S homeolog
, activin receptor like kinase-2