BMPR1B(bone morphogenetic protein receptor, type IB), also known as ALK6, is a a member of the bone morphogenetic protein (BMP) receptor family. BMPs are involved in endochondral bone formation and embryogenesis. These proteins transduce their signals through the formation of heteromeric complexes of 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding. BMPR1B is the major transducer of signals in precartilaginous condensations as demonstrated in experiments using constitutively active BMPR1B receptors. BMPR1B is a more effective trasducer of GDF5 than BMPR1A. Unlike BMPR1A null mice, which die at an early embryonic stage, BMPR1B null mice are viable.
ALK-3 is a type I receptor for bone morphogenetic proteins (BMPs) which belong to the protein kinase superfamily, TKL Ser/Thr protein kinase family and TGFB receptor subfamily. The BMP receptors consists of the type I receptors BMPR1A and BMPR1B and the type I I receptor BMPR2. Seven known type I serine/threonine kinases and five mammalian type II serine/threonine kinase receptors function in TGF-beta superfamily signal transduction. The downstream molecules of the type I BMP receptors include the Smad (Smad1, 5 and 8) proteins that are phosphorylated in a ligand-dependent manner, and relay the BMP signal from the receptors to target genes in the nucleus. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. ALK-3 contains a GS domain and a protein kinase domain. ALK-3 is widely expressed. Defects in BMPR1A gene are a cause of a significant proportion of cases of Juvenile polyposis syndrome (JPS).
Activin receptor-Like Kinase 3 (ALK-3), also known as Bone Morphogenetic Protein Receptor, type IA (BMPR1A), is a type I receptor for bone morphogenetic proteins (BMPs) which belong to the transforming growth factor beta (TGFB) superfamily. The BMP receptors form a subfamily of transmembrane serine/threonine kinases including the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. ALK-3/BMPR1A is expressed in the epithelium during branching morphogenesis. Deletion of BMPR1A in the epithelium with an Sftpc-cre transgene leads to dramatic defects in lung development. ALK-3 and ALK-6 share a high degree of homology, yet possess distinct signaling roles. The transforming growth factor (TGF)-beta type III receptor (TbetaRIII) enhanced both ALK-3 and ALK-6 signaling. ALK-3 plays an essential role in the formation of embryonic ventral abdominal wall, and abrogation of BMP signaling activity due to gene mutations in its signaling components could be one of the underlying causes of omphalocele at birth. The type IA BMP receptor, ALK-3 was specifically required at mid-gestation for normal development of the trabeculae, compact myocardium, interventricular septum, and endocardial cushion. Cardiac muscle lacking ALK-3 was specifically deficient in expressing TGFbeta2, an established paracrine mediator of cushion morphogenesis. Hence, ALK-3 is essential, beyond just the egg cylinder stage, for myocyte-dependent functions and signals in cardiac organogenesis.
Bone sialoprotein 2(IBSP) is a monomeric non-collagenous member of the SIBLING family of extracellular matrix proteins. It is principally associated with the early stages of bone mineralization. Mouse IBSP is synthesized as a 324 amino acid (aa) precursor that contains a 16 aa signal sequence and a 308 aa mature region. The mature segment is divided into a basic N-terminus (aa 17 - 62), a central region (aa 63 - 233), and an acidic C-terminus (aa 234 - 317). IBSP is highly glycosylated, sulfated and phosphorylated. Phosphorylation promotes HAp nucleation, while carbohydrate may regulate cell adhesion. IBSP binds tightly to hydroxyapatite, appears to form an integral part of the mineralized matrix. It is probably important to cell-matrix interaction and promotes Arg-Gly-Asp-dependent cell attachment.
Required for correct progression through G2 phase of the cell cycle and entry into mitosis. Required for RCOR1/CoREST mediated repression of neuronal specific gene promoters.Ubiquitously expressed in adult tissues. Contains 1 HMG box DNA-binding domain.
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