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Gene Review

Tpst1  -  protein-tyrosine sulfotransferase 1

Mus musculus

Synonyms: Protein-tyrosine sulfotransferase 1, R75054, TPST-1, Tango13a, Tyrosylprotein sulfotransferase 1
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Disease relevance of Tpst1

  • Tpst1(-/-) mice appear healthy but have approximately 5% lower average body weight than Tpst1(+/+) controls [1].
  • In addition, we show that although fertility of Tpst1(-/-) males and females per se is normal, Tpst1(-/-) females have significantly smaller litters because of fetal death between 8.5 and 15.5 days postcoitum [1].
  • This indicates that TPST1 and TPST2 have distinct macromolecular substrate specificities and provides clues as to the molecular mechanism of the infertility of Tpst2(-/-) males [2].

High impact information on Tpst1

  • Protein tyrosine O-sulfation is a post-translational modification mediated by one of two Golgi tyrosylprotein sulfotransferases (TPST1 and TPST2) that catalyze the transfer of sulfate to tyrosine residues in secreted and transmembrane proteins [2].
  • Tyrosine sulfation is mediated by one of two Golgi isoenzymes, called tyrosylprotein sulfotransferases (TPST-1 and TPST-2) [1].
  • To gain insight into the structural requirements for tyrosine sulfation in vivo, we have constructed and expressed an artificial gene encoding a polypeptide substrate for tyrosylprotein sulfotransferase [3].
  • In the accompanying paper (Friederich, E., Baeuerle, P. A., Garoff, H., Hovemann, B., and Huttner, W. B. (1988) J. Biol. Chem. 263, 14930-14938), we report on the expression of Drosophila yolk protein 2 in mouse fibroblasts and show the in vivo sulfation of tyrosine 172 by the vertebrate tyrosylprotein sulfotransferase [4].

Biological context of Tpst1

  • Our findings also strongly support the conclusion that TPST-1 and TPST-2 have distinct biological roles that may reflect differences in their macromolecular substrate specificity [1].


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