| First Author | Ilani T | Year | 2023 |
| Journal | EMBO J | Volume | 42 |
| Issue | 2 | Pages | e111869 |
| PubMed ID | 36245281 | Mgi Jnum | J:334089 |
| Mgi Id | MGI:7430652 | Doi | 10.15252/embj.2022111869 |
| Citation | Ilani T, et al. (2023) The disulfide catalyst QSOX1 maintains the colon mucosal barrier by regulating Golgi glycosyltransferases. EMBO J 42(2):e111869 |
| abstractText | Mucus is made of enormous mucin glycoproteins that polymerize by disulfide crosslinking in the Golgi apparatus. QSOX1 is a catalyst of disulfide bond formation localized to the Golgi. Both QSOX1 and mucins are highly expressed in goblet cells of mucosal tissues, leading to the hypothesis that QSOX1 catalyzes disulfide-mediated mucin polymerization. We found that knockout mice lacking QSOX1 had impaired mucus barrier function due to production of defective mucus. However, an investigation on the molecular level revealed normal disulfide-mediated polymerization of mucins and related glycoproteins. Instead, we detected a drastic decrease in sialic acid in the gut mucus glycome of the QSOX1 knockout mice, leading to the discovery that QSOX1 forms regulatory disulfides in Golgi glycosyltransferases. Sialylation defects in the colon are known to cause colitis in humans. Here we show that QSOX1 redox control of sialylation is essential for maintaining mucosal function. |
