دورية أكاديمية

SLC35A5 Protein—A Golgi Complex Member with Putative Nucleotide Sugar Transport Activity

التفاصيل البيبلوغرافية
العنوان: SLC35A5 Protein—A Golgi Complex Member with Putative Nucleotide Sugar Transport Activity
المؤلفون: Paulina Sosicka, Bożena Bazan, Dorota Maszczak-Seneczko, Yauhen Shauchuk, Teresa Olczak, Mariusz Olczak
المصدر: International Journal of Molecular Sciences, Vol 20, Iss 2, p 276 (2019)
بيانات النشر: MDPI AG, 2019.
سنة النشر: 2019
المجموعة: LCC:Biology (General)
LCC:Chemistry
مصطلحات موضوعية: nucleotide sugar transporters, Golgi apparatus, glycosylation, Biology (General), QH301-705.5, Chemistry, QD1-999
الوصف: Solute carrier family 35 member A5 (SLC35A5) is a member of the SLC35A protein subfamily comprising nucleotide sugar transporters. However, the function of SLC35A5 is yet to be experimentally determined. In this study, we inactivated the SLC35A5 gene in the HepG2 cell line to study a potential role of this protein in glycosylation. Introduced modification affected neither N- nor O-glycans. There was also no influence of the gene knock-out on glycolipid synthesis. However, inactivation of the SLC35A5 gene caused a slight increase in the level of chondroitin sulfate proteoglycans. Moreover, inactivation of the SLC35A5 gene resulted in the decrease of the uridine diphosphate (UDP)-glucuronic acid, UDP-N-acetylglucosamine, and UDP-N-acetylgalactosamine Golgi uptake, with no influence on the UDP-galactose transport activity. Further studies demonstrated that SLC35A5 localized exclusively to the Golgi apparatus. Careful insight into the protein sequence revealed that the C-terminus of this protein is extremely acidic and contains distinctive motifs, namely DXEE, DXD, and DXXD. Our studies show that the C-terminus is directed toward the cytosol. We also demonstrated that SLC35A5 formed homomers, as well as heteromers with other members of the SLC35A protein subfamily. In conclusion, the SLC35A5 protein might be a Golgi-resident multiprotein complex member engaged in nucleotide sugar transport.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1422-0067
Relation: http://www.mdpi.com/1422-0067/20/2/276; https://doaj.org/toc/1422-0067
DOI: 10.3390/ijms20020276
URL الوصول: https://doaj.org/article/13fecb41e56449e9bddba94448b0d960
رقم الأكسشن: edsdoj.13fecb41e56449e9bddba94448b0d960
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:14220067
DOI:10.3390/ijms20020276