Studies with a Xenopus BMP receptor suggest that ventral mesoderm-inducing signals override dorsal signals in vivo

Graff, Jonathan M.; Thies, R. Scott; Song, Jun Tae; Celeste, Anthony J.; Melton, Douglas A.

doi:10.1016/0092-8674(94)90409-x

Cited by 452 publications

(272 citation statements)

References 61 publications

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“…To elucidate the involvement of BMPR-IA in the BMP-2 signaling in C2C12 cells, a kinase domain-truncated BMPR-IA was constructed and stably transfected into C2C12 cells. This truncated BMPR-IA acts as a dominant negative receptor for BMP-4 signaling in the Xenopus embryo (23,34,35). When the kinase domain-truncated BMPR-IA was overexpressed in C2C12 myoblasts, they differentiated into MHC-positive myotubes but not into osteoblastlike ALP-positive cells, even in the presence of BMP-2.…”

Section: Discussionmentioning

confidence: 99%

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A Kinase Domain-truncated Type I Receptor Blocks Bone Morphogenetic Protein-2-induced Signal Transduction in C2C12 Myoblasts

Namiki

Akiyama

Katagiri

et al. 1997

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

“…A kinase domain-truncated BMPR-IA abolished the ventralizing activity of BMP-4 in a dominant negative manner in the Xenopus embryo (23,34,35). We therefore examined whether a dominant negative BMP type I receptor could inhibit the BMP-2-induced signalings in myoblasts.…”

mentioning

confidence: 99%

A Kinase Domain-truncated Type I Receptor Blocks Bone Morphogenetic Protein-2-induced Signal Transduction in C2C12 Myoblasts

Namiki

Akiyama

Katagiri

et al. 1997

Journal of Biological Chemistry

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“…When BMP4 was overexpressed in Xenopus embryos, the result was a striking ventralization and abolition of the Organizer (Jones et al, 1992;Dale et al, 1992). Expression of a dominant-negative mutated form of BMP receptor correspondingly blocked ventral development and induced partial ectopic axes when the RNA was injected on the ventral side (Graff et al, 1994). Thus, it was clear that BMPs act during gastrula stages to limit the dorsalizing effects of the Organizer.…”

Section: Morphogens In Vivo Part Ii: Fgfs and Bmpsmentioning

confidence: 99%

Morphogen gradients, positional information, and Xenopus: Interplay of theory and experiment

Green

2002

Developmental Dynamics

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The idea of morphogen gradients has long been an important one in developmental biology. Studies with amphibians and with Xenopus in particular have made significant contributions to demonstrating the existence, identity, and mechanisms of action of morphogens. Mesoderm induction and patterning by activin, nodals, bone morphogenetic proteins, and fibroblast growth factors have been analyzed thoroughly and reveal recurrent and combinatorial roles for these protein growth factor morphogens and their antagonists. The dynamics of nodal-type signaling and the intersection of VegT and ␤-catenin intracellular gradients reveal detailed steps in early long-range patterning. Interpretation of gradients requires sophisticated mechanisms for sharpening thresholds, and the activin-Xbra-Gsc system provides an example of this. The understanding of growth factor signal transduction has elucidated growth factor morphogen action and provided tools for dissecting their direct longrange action and distribution. The physical mechanisms of morphogen gradient establishment are the focus of new interest at both the experimental and theoretical level. General themes and emerging trends in morphogen gradient studies are discussed.

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“…The same mutant receptor also blocks the ventralizing and epidermalizing activity of TGF-␤ superfamily member BMP4 (11,13). BMP4 is expressed zygotically (i.e., after midblastula stages) on the ventral side of the embryo and has been implicated in ventralization of mesoderm and epidermalization of ectoderm (11,14). However, it is possible to block activin alone: a new activin receptor dominant-negative mutant, comprising only the extracellular domain, has been shown to cause dorsal disruptions without affecting ventral patterning or significantly reducing BMP4 responsiveness (15).…”

mentioning

confidence: 99%

Anteroposterior neural tissue specification by activin-induced mesoderm

Green

Cook

Smith

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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The transforming growth factor ␤ superfamily member, activin, is able to induce mesodermal tissues in animal cap explants from Xenopus laevis blastula stage embryos. Activin can act like a morphogen of the dorsoventral axis in that lower doses induce more ventral, and higher doses more dorsal, tissue types. Activin has also previously been reported to induce neural tissues in animal caps. From cell mixing experiments it was inferred that this might be an indirect effect of induced mesoderm signaling to uninduced ectoderm. Here we demonstrate directly that neural tissues do indeed arise by the action of induced mesoderm on uninduced ectoderm. Dorsal mesoderm is itself subdivided into posterior and anterior domains in vivo, but this had not been demonstrated for induced mesoderm. We therefore tested whether different concentrations of activin recreate these different anteroposterior properties as well. We show that the anteroposterior positional value of induced mesoderm, including its neuroinductive properties, depends on the dose of activin applied to the mesoderm, with lower doses inducing more posterior and higher doses giving more anterior markers. We discuss the implications of these results for patterning signals and the relationship between anteroposterior and dorsoventral axes.

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Studies with a Xenopus BMP receptor suggest that ventral mesoderm-inducing signals override dorsal signals in vivo

Cited by 452 publications

References 61 publications

A Kinase Domain-truncated Type I Receptor Blocks Bone Morphogenetic Protein-2-induced Signal Transduction in C2C12 Myoblasts

A Kinase Domain-truncated Type I Receptor Blocks Bone Morphogenetic Protein-2-induced Signal Transduction in C2C12 Myoblasts

Morphogen gradients, positional information, and Xenopus: Interplay of theory and experiment

Anteroposterior neural tissue specification by activin-induced mesoderm

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