Authors: | Mahony, D.; Weis, F. M. B.; Massagué, J.; Gurdon, J. B. |
Article Title: | XTrR-I is a TGFβ receptor and overexpression of a truncated form of the receptor inhibits axis formation and dorsalising activity |
Abstract: | We have previously cloned a type I serine/threonine kinase receptor from Xenopus, namely XTrR-I. We show here that XTrR-I is able to bind and mediate the activity of TGFβI, but is unable to mediate response to activin or BMP- 4. We have made a truncated receptor construct that can act as a dominant negative mutant receptor, and this can block the activity of TGFβ2 but not that of activin. Overexpression of either the full-length or truncated receptor has a drastic effect on mesoderm differentiation. The truncated receptor inhibits expression of notochord and muscle in mesodermalised animal caps, while the full-length receptor greatly increases the amount of notochord. In addition, the truncated receptor blocks the axis duplicating activity of both siamois and Xwnt8. We conclude that XTrR-I is involved in mediating a dorsalising activity important for mesoderm differentiation. |
Keywords: | protein expression; gene deletion; genetics; mutation; review; nonhuman; animal; metabolism; animals; gene expression; bone morphogenetic protein; transforming growth factor beta; embryo development; morphogenesis; cell differentiation; drug effect; physiology; animal embryo; gene expression regulation; prenatal development; embryo, nonmammalian; gene expression regulation, developmental; chemistry; messenger rna; rna, messenger; transforming growth factor beta receptor; receptors, transforming growth factor beta; protein family; mesoderm; body patterning; receptor density; muscle; muscles; xenopus; gastrulation; bone morphogenetic proteins; inhibin; receptor upregulation; bone morphogenetic protein 4; notochord; chromosome nor; blastula; activin; activins; priority journal; article; inhibins; siamois; xtrr i receptor; xtrr-i receptor; amphibia |
Journal Title: | Mechanisms of Development |
Volume: | 75 |
Issue: | 1-2 |
ISSN: | 0925-4773 |
Publisher: | Elsevier Science, Inc. |
Date Published: | 1998-07-01 |
Start Page: | 95 |
End Page: | 105 |
Language: | English |
DOI: | 10.1016/s0925-4773(98)00092-6 |
PUBMED: | 9739114 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Review -- Export Date: 12 December 2016 -- Source: Scopus |