| General information | Literature | Expression | Regulation | Mutation | Interaction |
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Basic Information |
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|---|---|
Gene ID | 9486 |
Name | CHST10 |
Synonymous | HNK-1ST|HNK1ST;carbohydrate sulfotransferase 10;CHST10;carbohydrate sulfotransferase 10 |
Definition | HNK-1 sulfotransferase|huHNK-1ST |
Position | 2q11.2 |
Gene type | protein-coding |
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Title |
Abstract |
| Human natural killer-1 sulfotransferase (HNK-1ST)-induced sulfate transfer regulates laminin-binding glycans on alpha-dystroglycan. | Retinoic acid (RA) is a well established anti-tumor agent inducing differentiation in various cancer cells. Recently, a robust up-regulation of human natural killer-1 sulfotransferase (HNK-1ST) was found in several subsets of melanoma cells during RA-mediated differentiation. However, the molecular mechanism underlying the tumor suppression mediated by HNK-1ST remains unclear. Here, we show that HNK-1ST changed the glycosylation state and reduced the ligand binding activity of alpha-dystroglycan (alpha-DG) in RA-treated S91 melanoma cells, which contributed to an attenuation of cell migration. Knockdown of HNK-1ST restored the glycosylation of alpha-DG and the migration of RA-treated S91 cells, indicating that HNK-1ST functions through glycans on alpha-DG. Using CHO-K1 cells, we provide direct evidence that HNK-1ST but not other homologous sulfotransferases (C4ST1 and GalNAc4ST1) suppresses the glycosylation of alpha-DG. The activity-abolished mutant of HNK-1ST did not show the alpha-DG-modulating function, indicating that the sulfotransferase activity of HNK-1ST is essential. Finally, the HNK-1ST-dependent incorporation of [(35)S]sulfate groups was detected on alpha-DG. These findings suggest a novel role for HNK-1ST as a tumor suppressor controlling the functional glycans on alpha-DG and the importance of sulfate transfer in the glycosylation of alpha-DG. |