Animal-vegetal asymmetries influence the earliest steps in retina fate commitment in Xenopus.
An individual retina descends from a restricted and invariant group of nine animal blastomeres at the 32-cell stage. We tested which molecular signaling pathways are responsible for the competence of animal blastomeres to contribute to the retina. Inactivation of activin/Vg1 or fibroblast growth factor (FGF) signaling by expression of dominant-negative receptors does not prevent an animal blastomere from contributing to the retina. However, increasing bone morphogenetic protein (BMP) signaling in the retina-producing blastomeres significantly reduces their contribution. Conversely, reducing BMP signaling by expression of a dominant-negative BMP receptor or Noggin allows other animal blastomeres to contribute to the retina. Thus, the initial step in the retinal lineage is regulated by position within the BMP/Noggin field of epidermal versus neural induction. Vegetal tier blastomeres, in contrast, cannot contribute to the retina even when given access to the appropriate position and signaling fields by transplantation to the dorsal animal pole. We tested whether expression of molecules within the mesoderm inducing (activin, FGF), mesoderm-modifying (Wnt), or neural-inducing (BMP, Noggin) pathways impart a retinal fate on vegetal cell descendants. None of these, several of which induce secondary head structures, caused vegetal cells to contribute to retina. This was true even if the injected blastomeres were transplanted to the dorsal animal pole. Two pathways that specifically induce head tissues also were investigated. The simultaneous blockade of Wnt and BMP signaling, which results in the formation of a complete secondary axis with head and eyes, did not cause the vegetal clone to give rise to retina. However, Cerberus, a secreted protein that also induces an ectopic head with eyes, redirected vegetal progeny into the retina. These experiments indicate that vegetal blastomere incompetence to express a retinal fate is not due to a lack of components of known signaling pathways, but relies on a specific pathway of head induction.
Moore
K B
KB
Department of Anatomy and Cell Biology, Institute for Biomedical Sciences, The George Washington University Medical Center, 2300 Eye Street NW, Ross Hall, Washington, DC, 20037, USA.
Moody
S A
SA
D028341:Activins; D000818:Animals; D030801:Animals, Genetically Modified; D001757:Blastomeres / Q000378:metabolism; D019485:Bone Morphogenetic Proteins / Q000378:metabolism; D002352:Carrier Proteins; D019070:Cell Lineage; D004627:Embryonic Induction; D005346:Fibroblast Growth Factors / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental; D006023:Glycoproteins / Q000378:metabolism; D007265:Inhibins / Q000378:metabolism; D008648:Mesoderm / Q000378:metabolism; D008954:Models, Biological; D011506:Proteins / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D012160:Retina / Q000166:cytology / Q000196:embryology*; D015398:Signal Transduction; D016212:Transforming Growth Factor beta; D051153:Wnt Proteins; D014981:Xenopus / Q000196:embryology* / Q000235:genetics; D029867:Xenopus Proteins; D029961:Zebrafish Proteins; D000099176:Noggin Protein
D028341:Activins; D019485:Bone Morphogenetic Proteins; D002352:Carrier Proteins; D005346:Fibroblast Growth Factors; D006023:Glycoproteins; D007265:Inhibins; D011506:Proteins; D011518:Proto-Oncogene Proteins; D016212:Transforming Growth Factor beta; D051153:Wnt Proteins; D029867:Xenopus Proteins; D029961:Zebrafish Proteins; D000099176:Noggin Protein; C513103:GDF1 protein, Xenopus