Handbook of Glycosyltransferases and Related Genes pp 1379-1391 | Cite as
Adenosine 3′-Phospho 5′-Phosphosulfate Transporter 1,2 (PAPST1,2) (SLC35B2,3)
Sulfation is one of the most important post-translational modifications of proteins and glycans as it generates sulfated molecules that are involved in a variety of biological processes. Sulfation is carried out in the lumen of the Golgi apparatus by a range of sulfotransferases. An activated form of sulfate, 3′-phosphoadenosine 5′-phosphosulfate (PAPS), is a common sulfate donor. Sulfotransferases transfer sulfate from PAPS to a defined position on a target sugar residue or Tyr residue. In higher organisms, PAPS is synthesized in the cytosol by a PAPS synthetase. PAPS transporters (PAPSTs), which are localized in the Golgi membrane, transport PAPS from the cytosol into the lumen of the Golgi apparatus by coupling with the antiport of adenosine 3′, 5′-diphosphate. Therefore, expression of PAPSTs determines the sulfation status of molecules on the cell surface and of secreted molecules.
To date, two PAPSTs, named PAPST1 and PAPST2, have been cloned and their activities identified. PAPST1 and PAPST2 are categorized as the second and third members of subgroup B of Solute carrier family 35 (SLC35B2 and SLC35B3, respectively). PAPST1 proteins have been identified from their PAPS transport activity in four mammalian species, the zebrafish and two invertebrate species, while PAPST2 proteins have been identified in two mammalian and two invertebrate species. Functional analyses of PAST1 and PAPST2 in model organisms and mammalian cells have shown that they have heparan sulfate-related or chondroitin sulfate-related activities. However, direct evidence linking defects in the activities of these transporter proteins to human disease has not been obtained to date.
KeywordsBone Morphogenetic Protein Golgi Apparatus Heparan Sulfate Chondroitin Sulfate Zebra Fish
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