Abstract
Of the many known covalent modifications of proteins1, few have been recognized as widespread. Among these modifications, protein phosphorylation has been extensively studied2–4. Recently, phosphorylation of tyrosine residues has been implicated in regulatory events such as cell transformation and hormone-induced cell growth5–7. The present study explores the possibility that another modification of tyrosine residues in proteins, tyrosine sulphation, may be widespread. This modification is particularly interesting because of the molecular resemblance of tyrosine-O-sulphate and tyrosine-O-phosphate. Protein sulphation on tyrosine residues was found to occur in all cell types in culture and all tissues in situ so far examined. Moreover, for each cell type and tissue, proteins containing tyrosine-O-sulphate were found in distinct electrophoretic patterns throughout the molecular weight range studied. Thus, protein sulphation on tyrosine residues appears to be a widespread covalent modification, and may have an important role in cell function.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Wold, F. A. Rev. Biochem. 50, 783–814 (1981).
Greengard, P. Science 199, 146–152 (1978).
Krebs, E. G. & Beavo, J. A. A. Rev. Biochem. 48, 923–959 (1979).
Cohen, P. in Molecular Aspects of Cellular Regulation Vol. 1 (ed. Cohen, P.) 255–268 (North-Holland, Amsterdam, 1980).
Hunter, T. Cell 22, 647–648 (1980).
Erikson, R. L., Purchio, A. F., Erikson, E., Collett, M. S. & Brugge, J. S. J. Cell Biol. 87, 319–325 (1980).
Ushiro, H. & Cohen, S. J. biol. Chem. 255, 8363–8365 (1980).
Reitz, H. C., Ferrel, R. E., Fraenkel-Conrat, H. & Olcott, H. S. J. Am. chem. Soc. 68, 1024–1031 (1946).
Bettelheim, F. R. J. Am. chem. Soc. 76, 2838–2839 (1954).
Cleveland, D. W., Fischer, S. G., Kirschner, M. W. & Laemmli, U. K. J. biol. Chem. 252, 1102–1106 (1977).
Gregory, H., Hardy, P. M., Jones, D. S., Kenner, G. W. & Sheppard, R. C. Nature 204, 931–933 (1964).
Anastasi, A., Bertaccini, G. & Erspamer, V. Br. J. Pharmac. Chemother. 27, 479–485 (1966).
Anastasi, A., Erspamer, V. & Endean, R. Experientia 23, 699–700 (1967).
Mutt, V. & Jorpes, J. E. Eur. J. Biochem. 6, 156–162 (1968).
Unsworth, C. D., Hughes, J. & Morley, J. S. Nature 295, 519–522 (1982).
Laemmli, U. K. Nature 227, 680–685 (1970).
Huttner, W. B. & Greengard, P. Proc. natn. Acad. Sci. U.S.A. 76, 5402–5406 (1979).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Huttner, W. Sulphation of tyrosine residues—a widespread modification of proteins. Nature 299, 273–276 (1982). https://doi.org/10.1038/299273a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/299273a0
This article is cited by
-
Enhanced tyrosine sulfation is associated with chronic kidney disease-related atherosclerosis
BMC Biology (2023)
-
Phytosulfokine promotes cell division in protoplast culture and adventitious shoot formation in protoplast-derived calluses of Nicotiana benthamiana
Plant Biotechnology Reports (2022)
-
Using circulating O-sulfotyrosine in the differential diagnosis of acute kidney injury and chronic kidney disease
BMC Nephrology (2021)
-
Rapid and efficient protein synthesis through expansion of the native chemical ligation concept
Nature Reviews Chemistry (2018)
-
Direct Identification of Tyrosine Sulfation by using Ultraviolet Photodissociation Mass Spectrometry
Journal of the American Society for Mass Spectrometry (2014)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.