A Mammalian Serine/Threonine Kinase Receptor Specifically Binds BMP-2 and BMP-4

Yamaji, Noboru; Celeste, Anthony J.; Thies, R. Scott; Song, Jingwen; Bernier, Suzanne M.; Goltzman, David; Lyons, Karen M.; Nove, John; Rosen, Vicki; Wozney, John M.

doi:10.1006/bbrc.1994.2898

Cited by 79 publications

(52 citation statements)

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“…Another type I BMP-2/4 receptor CFK-43a (also known as ALK-6) is expressed in a more restricted pattern, may provide a compensatory signaling pathway for mesoderm formation in Bmpr mutant embryos when grown in the testes (ten Dijke et al 1994;Yamaji et al 1994;Dewulf et al 1995). One consistent finding from the testicular transplant experiments was the impaired growth of the mutant embryos in comparison with the normal embryos, suggesting a deficit in cell proliferation potential that is independent of mesoderm formation {i.e., even the mesoderm that forms in the tumors appears to grow slowly, so the proliferation defect is not confined only to mutant epiblast cellsl.…”

Section: Roles For Bmp-2/4 Receptor Signalingmentioning

confidence: 99%

Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis.

Mishina¹,

Suzuki²,

Ueno³

et al. 1995

Genes Dev.

725

543

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Bone morphogenetic proteins (BMPs) are secreted proteins that interact with cell-surface receptors and are believed to play a variety of important roles during vertebrate embryogenesis. Bmpr, also known as ALK-3 and Brk-1, encodes a type I transforming growth factor-~ (TGF-[3) family receptor for BMP-2 and BMP-4. Bmpr is expressed ubiquitously during early mouse embryogenesis and in most adult mouse tissues. To study the function of Bmpr during mammalian development, we generated Bmpr-mutant mice. After embryonic day 9.5 (E9.5), no homozygous mutants were recovered from heterozygote matings. Homozygous mutants with morphological defects were first detected at E7.0 and were smaller than normal. Morphological and molecular examination demonstrated that no mesoderm had formed in the mutant embryos. The growth characteristics of homozygous mutant blastocysts cultured in vitro were indistinguishable from those of controls; however, embryonic ectoderm (epiblast) cell proliferation was reduced in all homozygous mutants at E6.5 before morphological abnormalities had become prominent. Teratomas arising from E7.0 mutant embryos contained derivatives from all three germ layers but were smaller and gave rise to fewer mesodermal cell types, such as muscle and cartilage, than controls. These results suggest that signaling through this type I BMP-2/4 receptor is not necessary for preimplantation or for initial postimplantation development but may be essential for the inductive events that lead to the formation of mesoderm during gastrulation and later for the differentiation of a subset of mesodermal cell types.

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Section: Roles For Bmp-2/4 Receptor Signalingmentioning

confidence: 99%

Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis.

Mishina¹,

Suzuki²,

Ueno³

et al. 1995

Genes Dev.

725

543

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“…Furthermore, the contrasting findings between activin and BMP-2 and BMP-4 ligand mutant mice and mice mutant for their respective receptors may also be attributable in part to crosstalk between ligands and receptors. TGF-f3 family ligands are structurally related to each other (Kingsley 1994) and it has been shown that one type of receptor can interact with several classes of ligands (Attisano et al 1993;Koenig et al 1994;Suzuki et al 1994;ten Dijke et al 1994;Yamaji et al 1994). In addition, other studies indicate that one ligand can interact with several classes of receptors (Attisano et al 1992(Attisano et al , 1993ten Dijke et al 1994).…”

Section: The Simplicity Of the Mis Signaling Pathway Relative To The mentioning

confidence: 99%

Genetic analysis of the Müllerian-inhibiting substance signal transduction pathway in mammalian sexual differentiation.

Mishina¹,

Rey²,

Finegold³

et al. 1996

Genes Dev.

338

212

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“…To date, four other mammalian type II receptors have been identified: ActRIIB (Attisano et al 1992), AMHR-II (Baarends et al 1994, di Clemente et al 1994, TbRII (Lin et al 1992), and BMPRII (Kawabata et al 1995, Liu et al 1995, Nohno et al 1995, Rosenzweig et al 1995. In addition, seven type I receptors termed activin receptor-like kinase (ALK)-1 to ALK-7 have also been cloned , ten Dijke et al 1993, Tsuchida et al 1993, 1996, Yamaji et al 1994. Nonetheless, receptors within type I and type II classes differ in affinity and specificity, and may be expressed differentially to allow triggering of different components of the intracellular-signaling cascade.…”

Section: Introductionmentioning

confidence: 99%

The structural basis of TGF-β, bone morphogenetic protein, and activin ligand binding

Lin¹,

Lerch²,

Cook³

et al. 2006

Reproduction

125

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The transforming growth factor-b (TGF-b) superfamily is a large group of structurally related growth factors that play prominent roles in a variety of cellular processes. The importance and prevalence of TGF-b signaling are also reflected by the complex network of check points that exist along the signaling pathway, including a number of extracellular antagonists and membranelevel signaling modulators. Recently, a number of important TGF-b crystal structures have emerged and given us an unprecedented clarity on several aspects of the signal transduction process. This review will highlight these latest advances and present our current understanding on the mechanisms of specificity and regulation on TGF-b signaling outside the cell.

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A Mammalian Serine/Threonine Kinase Receptor Specifically Binds BMP-2 and BMP-4

Cited by 79 publications

References 0 publications

Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis.

Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis.

Genetic analysis of the Müllerian-inhibiting substance signal transduction pathway in mammalian sexual differentiation.

The structural basis of TGF-β, bone morphogenetic protein, and activin ligand binding

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