Ask about this productRelated genes to: SURF4 antibody
- Gene:
- SURF4 NIH gene
- Name:
- surfeit 4
- Previous symbol:
- -
- Synonyms:
- ERV29, FLJ22993, MGC102753
- Chromosome:
- 9q34.2
- Locus Type:
- gene with protein product
- Date approved:
- 1989-11-29
- Date modifiied:
- 2016-10-05
Related products to: SURF4 antibody
Related articles to: SURF4 antibody
- Export of secretory proteins from the endoplasmic reticulum is mediated by the COPII coat which must accommodate diverse cargoes. While small COPII vesicles are well characterised, they do not explain ER exit of exceptionally large and abundant cargoes such as procollagens. Recent work has expanded the classic vesicular model of COPII-mediated secretion toward a more flexible view of the COPII coat architecture, in which cell- and cargo-specific regulators of coat turnover and membrane tethers can remodel ER exit sites (ERES) to meet cargo-specific demands. Multicellular organisms have evolved an expanded network of COPII paralogues and interacting proteins such as SURF4, TMEM proteins, and TANGO1 that may generate enlarged carriers, membrane tubules, or transient intercompartmental continuities for large cargo exit from the ER. This review highlights recent progress and remaining gaps in understanding how COPII is regulated to mediate ER export of large cargo and identifies priorities for future investigation. - Source: PubMed
Publication date: 2026/05/06
Phillips Patrick MorleyZanetti Giulia - YIPF5 is an ER-membrane protein implicated in ER-Golgi transport. Mutations in YIPF5 cause MEDS2 (microcephaly, epilepsy, and neonatal diabetes syndrome), a fatal disorder manifesting in early childhood. We demonstrate that YIPF5 is involved in ER export of a subset of proteins, including cargoes of the ER export receptor SURF4, with which it directly interacts. YIPF5 knockout cells display altered cell surface and secretome profiles, with reduced neuronal adhesion molecules and increased secretion of ER chaperones affecting migration. YIPF5 depletion enhances cell migration in a wound-healing assay and alters SURF4 localization, causing elongated ERGIC53- and Rab1-positive tubules from ER exit sites. Kinetic analysis suggests that YIPF5 negatively regulates SURF4-mediated ER export. knockdown of in embryonic mouse brains induces premature neuronal migration and abnormal neuronal morphology. Our findings suggest that YIPF5 and SURF4 coordinate ER export of key proteins and disruption may underlie cortical development defects leading to microcephaly. - Source: PubMed
Publication date: 2026/01/27
Bruno FrancescaAnitei MihaelaDi Fraia DomenicoDurso WilliamDau ThereseCirri EmilioSannai MaraValkova ChristinaMaldutyte JulijaMiller Elizabeth ARubio IgnacioGarloff VeraKersten NoortjeFarias Ginny GOri AlessandroMestres IvánCalegari FedericoKaether Christoph - Drug resistance, metastasis, and recurrence are major contributors to the poor survival rates of lung adenocarcinoma (LUAD) patients. Studies suggest that tumor stemness is a key driver of drug resistance, recurrence, and metastasis. Although Surfeit locus protein 4 (SURF4) has been shown to promote tumor cell stemness, the molecular mechanisms by which SURF4 regulates LUAD growth and stemness remain elusive. - Source: PubMed
Publication date: 2026/01/26
Zhou JunzhengNie ShiweiZheng XiaodongWei XudongZhang JinruiShen XiaojuanZhang Weimin - Subclinical ketosis in dairy cows is accompanied by adaptive changes in the secretory function of the mammary gland. However, the molecular basis underlying this adaptation remains unclear. The secretory capacity of the mammary gland is closely linked to the activation of the unfolded protein response (UPR) and endoplasmic reticulum (ER) biogenesis, particularly the inositol-requiring enzyme 1α (IRE1α) pathway. Thus, this study aims to investigate whether BHB activates the IRE1α-XBP1 signaling axis to promote ER biogenesis, thereby sustaining casein synthesis. In this study, MAC-T cells were treated with 1.8 mM BHB for 0, 12, 24, or 48 h to mimic subclinical ketotic conditions. We first observed that BHB activated all 3 branches of the UPR without inducing the proapoptotic element of the UPR. Meanwhile, MAC-T cells treated with BHB show a significant increase in ER tracker staining and upregulated mRNA levels of ER biogenesis-related genes, such as choline kinase alpha (CHKA), choline-phosphate cytidylyltransferase alpha (PCYT1A), and Surfeit 4 (SURF4). Subsequently, BHB upregulated the mRNA abundance of genes related to ribosome biogenesis and the proregenerative phenotype in MAC-T cells. The MAC-T cells treated with 1.8 mM BHB also displayed increased protein abundance of β-casein, along with the casein beta (CSN2), casein kappa (CSN3), casein alpha S1 (CSN1S1), and casein alpha S2 (CSN1S2) milk protein genes. Compared with the 1.8 mM BHB group, cotreatment with BHB and KIRA6 significantly suppressed the BHB-induced increase in ER tracker fluorescence, ER biogenesis-related gene expression, and β-casein protein abundance. Silencing XBP1 via small interfering RNA inhibited BHB-induced ER biogenesis and β-casein synthesis, whereas the overexpression of XBP1 alleviated these effects. Furthermore, under BHB treatment, overexpression of XBP1 partially attenuated the suppressive effects of IRE1α inhibition on ER biogenesis and β-casein synthesis. Overall, our data demonstrate that BHB promotes ER biogenesis and milk protein synthesis in mammary epithelial cells through activation of the IRE1α-XBP1 signaling pathway, suggesting a protective and adaptive role for BHB in maintaining mammary gland function under subclinical ketotic conditions. - Source: PubMed
Publication date: 2026/01/15
Cao LiguangHan JiatongLi GuojinLiu KaiGao WenruiYang ZifengDong YifeiDu YushanDu XiliangSong YuxiangLi XinweiLei LinGao WenwenLiu Guowen - Sonic hedgehog (Shh) signaling orchestrates diverse developmental processes in metazoans and is implicated in numerous human diseases. While downstream signaling in recipient cells have been extensively characterized, the mechanisms governing secretion of newly synthesized Shh from producer cells remain less well understood. Building on our previous identification of a Surfeit locus protein 4 (SURF4)-to-proteoglycan (PG) relay mechanism that mediates endoplasmic reticulum (ER)-to-Golgi transport of the N-terminal Shh fragment (ShhN), we investigated ShhN export from the trans-Golgi network (TGN). We show that ShhN exits the TGN via a clathrin-dependent secretory pathway. Mechanistic analyses identify the transmembrane protein glutamate receptor 1 (GRIA1) as a key mediator: GRIA1 associates with ShhN in Golgi-derived vesicles, physically interacts with ShhN, colocalizes with ShhN after TGN exit, and is required for efficient TGN export and secretion of ShhN. Notably, the Cardin-Weintraub (CW) motif on ShhN, previously shown to engage SURF4 for ER-to-Golgi trafficking, is also essential for TGN export, and PGs are critical for the GRIA1-ShhN interaction. Furthermore, GRIA1 regulates intracellular trafficking of endogenous full length Shh and modulates Shh pathway activity in Neuro-2a (N2A) cells. Together, these findings identify GRIA1 as an important regulator of Shh TGN export and advance our understanding of the molecular mechanisms that control Shh secretion. - Source: PubMed
Publication date: 2025/12/22
Tang XiaoTian YeWang QianyuanSong ZiyangZhao XiaoxuGuo Yusong