DDOST

Last update 08 May 2025

Basic Info

Synonyms

DDOST, DDOST 48 kDa subunit, Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit

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Introduction

Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (PubMed:22467853).

100 Clinical Results associated with DDOST

100 Translational Medicine associated with DDOST

0 Patents (Medical) associated with DDOST

Literatures (Medical) associated with DDOST

01 Mar 2025·Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology

Endocytosis, endoplasmic reticulum, actin cytoskeleton affected in tilapia liver under polystyrene microplastics and BDE153 acute co-exposure

Article

Author: Hu, Jiawen ; Zheng, Yao ; Li, Jiajia ; Xu, Gangchun ; Sun, Yi ; Zhu, Haojun

Studies showed that contaminants adhered to the surface of nano-polystyrene microplastics (NPs) have a toxicological effect. Juveniles tilapia were dispersed into four groups: the control group A, 75 nm NPs exposed group B, 5 ng·L^-1 2,2',4,4',5,5'-hexabromodiphenyl ether group C (BDE₁₅₃), and 5 ng·L^-1 BDE₁₅₃ + 75 nm MPs group D, and acutely exposed for 2, 4 and 8 days. The hepatic histopathological change, enzymatic activities, transcriptomics, and proteomics, have been performed in tilapia. The results showed that the enzymatic activities of anti-oxidative (ROS, SOD, EROD), energy (ATP), lipid metabolism (TC, TG, FAS, LPL, ACC), pro-inflammatory (TNFα, IL-1β) and apoptosis (caspase 3) significantly increased at 2 d in BDE₁₅₃ and the combined group and together in BDE₁₅₃ group at 8 d. Histological slice showed displaced nucleus by BDE₁₅₃ exposure and vacuoles appeared in the combined groups. KEGG results revealed that pathways associated with endocytosis, protein processing in endoplasmic reticulum and regulation of actin cytoskeleton were significantly enriched. The selected genes associated with neurocentral development (ganab, diaph3/baiap2a/ddost decreased and increased), lipid metabolism (ldlrap1a decreased, stt3b increased), energy (agap2 decreased, uggt1 increased) were affected under co-exposure, and fibronectin significantly increased via proteome. Our study indicated that endocytosis, protein processing in endoplasmic reticulum, regulation of actin cytoskeleton were affected in tilapia liver under NPs and BDE₁₅₃ co-exposure.

01 Feb 2025·Advanced Science

N‐glycosylation Modification of CTSD Affects Liver Metastases in Colorectal Cancer

Article

Author: Wang, Caihong ; Sun, Qing ; Gao, Zhidong ; Shen, Zhanlong ; Du, Yan ; Li, Yan ; Ye, Yingjiang ; Yan, Quanyi ; Zhan, Jun ; Xiong, Nan ; Zhang, Hongquan ; Wang, Shan ; Yang, Changjiang ; Huang, Chuncui ; Zhao, Long

AbstractLiver metastasis is the primary factor contributing to unfavorable prognosis in colorectal cancer (CRC). Although N‐glycosylation is implicated in metastasis, there is a notable paucity of comprehensive studies addressing the N‐glycosylation proteomics associated with liver metastasis in CRC. In this study, N‐glycosylated proteins and N‐glycosylation sites of differential expression between primary lesions and paired liver metastatic lesions are identified. Cathepsin D (CTSD) is further screened as a potentially pivotal N‐glycosylated protein in CRC liver metastasis. Glycosyltransferases complex DDOST and STT3B can regulate N‐glycosylation modification at residue 263 of CTSD (a protease), thereby affecting CTSD protease to lyse ACADM. ACADM can regulate ferroptosis‐related proteins (ACSL4, SLC7A11, and GPX4) to further influence the invasion and metastasis of CRC cells. This newly discovered mechanism provides potential therapeutic targets for CRC treatment and insights for controlling CRC progression and metastasis.

01 Dec 2024·Cellular and Molecular Life Sciences

ALKBH1 promotes HIF-1α-mediated glycolysis by inhibiting N-glycosylation of LAMP2A

Article

Author: Li, Jianshuang ; Liu, Xinjie ; Liu, Yanyan ; Hu, Liubing ; Guo, Haolin ; Zhou, Qinghua ; Li, Mengmeng ; Lin, Miao ; Tan, Junyang

AbstractALKBH1 is a typical demethylase of nucleic acids, which is correlated with multiple types of biological processes and human diseases. Recent studies are focused on the demethylation of ALKBH1, but little is known about its non-demethylase function. Here, we demonstrate that ALKBH1 regulates the glycolysis process through HIF-1α signaling in a demethylase-independent manner. We observed that depletion of ALKBH1 inhibits glycolysis flux and extracellular acidification, which is attributable to reduced HIF-1α protein levels, and it can be rescued by reintroducing HIF-1α. Mechanistically, ALKBH1 knockdown enhances chaperone-mediated autophagy (CMA)-mediated HIF-1α degradation by facilitating the interaction between HIF-1α and LAMP2A. Furthermore, we identify that ALKBH1 competitively binds to the OST48, resulting in compromised structural integrity of oligosaccharyltransferase (OST) complex and subsequent defective N-glycosylation of LAMPs, particularly LAMP2A. Abnormal glycosylation of LAMP2A disrupts lysosomal homeostasis and hinders the efficient degradation of HIF-1α through CMA. Moreover, NGI-1, a small-molecule inhibitor that selectively targets the OST complex, could inhibit the glycosylation of LAMPs caused by ALKBH1 silencing, leading to impaired CMA activity and disruption of lysosomal homeostasis. In conclusion, we have revealed a non-demethylation role of ALKBH1 in regulating N-glycosylation of LAMPs by interacting with OST subunits and CMA-mediated degradation of HIF-1α.

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DDOST

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