Regulation of TGF-β signalling by N-acetylgalactosaminyltransferase-like 1
Development, ISSN: 0950-1991, Vol: 135, Issue: 10, Page: 1813-1822
2008
- 33Citations
- 46Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations33
- Citation Indexes33
- CrossRef33
- 33
- Captures46
- Readers46
- 46
Article Description
The TGF-β superfamily of secreted signalling molecules plays a pivotal role in the regulation of early embryogenesis, organogenesis and adult tissue homeostasis. Here we report the identification of Xenopus N-acetylgalactosaminyltransferase-like 1 (xGaIntl-1) as a novel important regulator of TGF-β signalling. N-acetylgalactosaminyltransferases mediate the first step of mucin-type glycosylation, adding N-acetylgalactose to serine or threonine side chains. xGalntI-1 is expressed in the anterior mesoderm and neural crest territory at neurula stage, and in the anterior neural crest, notochord and the mediolateral spinal cord at tailbud stage. Inhibition of enfogenous xGaIntl-1 protein synthesis, using specific morpholino oligomers, interfered with the formation of anterior neural crest, anterior notochord and the spinal cord. Xenopus and mammalian GaIntl-1 inhibited Activin as well as BMP signalling in the early Xenopus embryo and in human HEK 293T cells. Gain- and loss-of-function experiments showed that xGaIntl-1 interferes with the activity of the common TGF-β type II receptor ActR-IIB in vivo. In addition, our biochemical data demonstrated that xGaIntI-1 specifically interferes with the binding of ActR-IIB to Activin- and BMP-specific type I receptors. This inhibitory activity of xGaIntI-1 was dependent on mucin-type glycosylation, as it was sensitive to the chemical inhibitor benzyl-GaINAc. These studies reveal an important role of a N-acetylgalactosaminyltransferase in the regulation of TGF-β signalling. This novel regulatory mechanism is evolutionarily conserved and, thus, might provide a new paradigm for the regulation of TGF-β signalling in vertebrates.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=49949092699&origin=inward; http://dx.doi.org/10.1242/dev.019323; http://www.ncbi.nlm.nih.gov/pubmed/18417620; https://journals.biologists.com/dev/article/135/10/1813/64673/Regulation-of-TGF-signalling-by-N; https://dx.doi.org/10.1242/dev.019323; https://dev.biologists.org/content/135/10/1813
The Company of Biologists
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