Ask about this productRelated genes to: SERINC3 antibody
- Gene:
- SERINC3 NIH gene
- Name:
- serine incorporator 3
- Previous symbol:
- TDE1
- Synonyms:
- DIFF33, TDE, SBBI99, TMS-1, AIGP1
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-07
- Date modifiied:
- 2014-11-19
Related products to: SERINC3 antibody
Related articles to: SERINC3 antibody
- SERINC3, a member of the serine incorporator protein family, is known for its roles in viral resistance and tumorigenesis, however, its function in osteogenesis remains unexplored. - Source: PubMed
Publication date: 2026/07/03
Zheng ZhichaoXu TianruPathak Janak LXu ShaofenLu JiaruiYu ShuiqingFu ZhiheXie WeiZhu HaohuiJaspers Richard TZheng HuadeWu LihongLi Jiang - Head and neck squamous cell carcinoma (HNSCC) was characterized by pronounced heterogeneity and therapeutic resistance, which posed challenges for effective clinical management. Regulated cell death (RCD) and cellular senescence (CS) were recognized as fundamental hallmarks of cancer, exerting effects on tumorigenesis, progression, and treatment sensitivity. However, the utility of cell death and cellular senescence (CDCS) in predicting prognosis and therapeutic response had not been fully established. - Source: PubMed
Publication date: 2026/05/22
Luo XiaoqinHe Xian - Serine incorporator 5 (SERINC5) restricts the infectivity of various enveloped viruses, including HIV-1 and severe acute respiratory syndrome coronavirus 2. However, these pandemic viral pathogens have evolved mechanisms to counteract this restriction. Here, we examined the impact of all five human SERINC family members on the seasonal human coronaviruses (hCoVs) 229E and OC43, which account for up to 15% of global mild respiratory infections and can cause severe disease in vulnerable individuals. Our data show that both exogenous and endogenous SERINC1, SERINC3, and SERINC5 significantly reduce OC43 infectivity in human lung and liver cells but have little, if any, effect on 229E. Functional analyses revealed that both the 130-amino-acid ORF4a protein encoded by most laboratory 229E strains and the full-length 219 amino acid ORF4 protein encoded by clinical 229E isolates antagonize SERINC5 by promoting its relocalization to lysosomes and subsequent degradation. Finally, we show that endogenous SERINC5 expression in primary human lung cells inhibits infection by ORF4-deficient but not wild-type hCoV-229E. In conclusion, several SERINC proteins restrict hCoV-OC43, whereas hCoV-229E efficiently counteracts SERINC-mediated restriction by its ORF4/4a accessory proteins to ensure efficient production of fully infectious viral particles. - Source: PubMed
Publication date: 2026/05/29
Xie QinyaNoettger SabrinaLawrenz JanStopper SophieKlute SusanneMünch JanKmiec DorotaWang QingxingSparrer Konstantin M JKirchhoff Frank - Human transmembrane proteins Serinc3 and Serinc5 are antiviral restriction factors that inhibit HIV-1 infectivity. In the absence of viral antagonism, Serinc3 and Serinc5 incorporate into the envelopes of nascent virions and inhibit the fusion of virions to the target cells. The HIV-1 virus counteracts the restriction of Serinc3 by downregulating it from the cell surface and thus excluding it from budding virions. This is orchestrated by the viral accessory protein Nef and involves hijacking of the clathrin adaptor protein complex 2 (AP2)-dependent endocytosis. The mechanistic details of Nef-mediated Serinc3 downregulation, however, have been enigmatic. In this work, we investigated and revealed the molecular determinants of Serinc3 modulation by Nef. Our results show that Nef recruits Serinc3 by binding to its N-terminal cytosolic tail. Furthermore, Nef residues important for Serinc3-binding in vitro, and for the exclusion of Serinc3 from virions, overlap with those required for Nef-mediated CD4 downregulation, suggesting great mechanistic similarities between the two functions of Nef. In addition to shedding light on the mechanism of Serinc3 antagonism, our work also highlights the conserved substrate-binding pocket of Nef as a molecular hotspot for inhibitor development and antiretroviral drug discovery. - Source: PubMed
Publication date: 2025/12/19
Karimian Shamsabadi MohammadStoneham CharlotteDe Leon AmaliaFares TonyGuatelli JohnJia Xiaofei - The HIV-1 restriction factor, hSERINC3, functions as a lipid scramblase, translocating lipids across the bilayer in reconstituted proteoliposomes and the viral envelope. Phosphatidylserine(PS) scrambling and exposure at the outer leaflet are recognized to play important roles in several biological processes. To understand the mechanistic basis for hSERINC3-mediated PS lipid scrambling at atomistic resolution, we implemented the transition-tempered metadynamics (TTMetaD) enhanced sampling method. Our simulations sampled close-to-open hSERINC3 conformational transition during PS scrambling and demonstrated that while other non-ATP-dependent lipid transporters with similar architecture transport lipid following a "trap-and-flip" mechanism, hSERINC3 adopts a "credit card" mechanism of lipid scrambling and does not follow the classical "alternating access" mechanism. Notably, we observe unfolding of the H8 NTD, consistent with the cryo-EM density map of WT-hSERINC3, mediates PS scrambling. A cluster of hydrophilic residues in the hSERINC3 central cavity, forming central gates and interacting with the PS headgroup, stabilizes the intermediate state of inner-groove scrambling and is also observed in the AlphaFold2 model of hSERINC5 that exhibits the highest viral restriction activity. Surprisingly, our simulations reveal distinct pathways for lipid translocation and pathway-dependent alterations of hSERINC3 central cavity, providing direct evidence for a non-canonical, closed-state out-of-groove PS scrambling in a complex membrane environment. - Source: PubMed
Publication date: 2025/11/13
Banerjee PujaYeager MarkVoth Gregory A