Ask about this productRelated genes to: SLC37A4 antibody
- Gene:
- SLC37A4 NIH gene
- Name:
- solute carrier family 37 member 4
- Previous symbol:
- G6PT1, G6PT2, G6PT3
- Synonyms:
- GSD1b, GSD1c, GSD1d
- Chromosome:
- 11q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-15
- Date modifiied:
- 2019-04-23
Related products to: SLC37A4 antibody
Related articles to: SLC37A4 antibody
- Genetic neutropenia comprises heterogeneous phenotypes with variable patterns and severity of infectious complications. However, comparative real-world data on subtype-specific infectious complications remain limited. We analysed patients with genetic neutropenia enrolled in the Canadian Inherited Marrow Failure Registry between 2001 and 2025. Patients were classified into severe congenital neutropenia (SCN), cyclic neutropenia, syndromic neutropenia or suspected genetic neutropenia (SGN). Infectious complications were classified by type and severity. Eighty-nine patients were included, including SCN (n = 27), cyclic neutropenia (n = 13), syndromic neutropenia (n = 25) and SGN (n = 24). Elastase, neutrophil expressed (ELANE) variants were most common (n = 30) and predominated in SCN and cyclic neutropenia, whereas syndromic neutropenia included tafazzin (TAZ), solute carrier family 37 member 4 (SLC37A4), vacuolar protein sorting 13 homolog B (VPS13B), C-X-C motif chemokine receptor 4 (CXCR4), glucose-6-phosphatase catalytic subunit 3 (G6PC3), signal recognition particle 54 (SRP54) and HCLS1 associated protein X-1 (HAX1) variants. Overall, 68 patients (76.4%) experienced ≥1 infectious complication and 45 (50.6%) developed severe infections. Febrile neutropenia occurred more frequently in SCN (59.3%) than in other subtypes (p = 0.005), while skin and soft tissue infections were more common in syndromic neutropenia (56.0%) and SCN (44.4%) (p = 0.038). Granulocyte colony-stimulating factor was administered in 60 patients, with an overall response rate of 90.0%. Ten patients underwent haematopoietic stem cell transplantation. Infection patterns differed across genetic neutropenia subtypes, supporting subtype-informed surveillance and management. - Source: PubMed
Publication date: 2026/09/30
Choi Young BaeAlshammari Nawaf R RMathew RinuLi HongbingCada MichaelaAbish SharonPastore Yves DSteele MacGregorKlaassen Robert JVilleneuve StephanieCorriveau-Bourque CatherineSinha RoonaRayar MeeraWheaton LauraBreakey VickyGoodyear LisaCrooks BruceTole SoumitraShim Ye JeeDror Yigal - Cogan's syndrome (CS) is a rare autoimmune disorder involving audio-vestibular and ocular inflammation. While systemic vasculitis is a known complication, its association with Moyamoya-type cerebrovascular remodeling has not been previously documented. A 19-year-old Asian woman was diagnosed with atypical CS following a presentation of hyperpyrexia, unintentional weight loss, and severe bilateral sensorineural hearing loss. After five years of appropriate immunosuppressive treatment, she developed subacute headaches, hypertension, and left hemiparesis and paresthesia. Despite normal inflammatory markers, neuroimaging revealed right-sided internal carotid artery occlusion and extensive collateralization characteristic of Moyamoya syndrome. Genetic testing showed a variant of uncertain significance in SLC37A4. The patient underwent a right extracranial-intracranial (STA-MCA) bypass, resulting in complete resolution of neurological symptoms. The late emergence of Moyamoya suggests that chronic autoimmune-mediated vascular injury may trigger progressive steno-occlusive disease. Clinicians should consider Moyamoya syndrome as a differential for new neurological symptoms in CS patients, even when systemic inflammation appears controlled. To our knowledge, this is the first reported case of concurrent Cogan's syndrome and Moyamoya vasculopathy at time of writing this article. - Source: PubMed
Publication date: 2026/07/07
Phu AmyChao EricaSood RanjanaChen David RAgrawal Devendra K - The endoplasmic reticulum glucose-6-phosphatase (G6Pase) system, traditionally linked to hepatic and renal glucose homeostasis, is increasingly recognized as a regulator of intracellular glucose-6-phosphate (G6P) partitioning with broad relevance to cancer biology. Emerging evidence implicates its catalytic subunits (G6PC1-3) and associated transporters, particularly SLC37A4/G6PT, in redox control, calcium homeostasis, protein quality control, glycogen metabolism, autophagy, epithelial-mesenchymal transition, stemness, immune evasion, and therapy resistance. In several non-gluconeogenic cancers, elevated G6Pase-system activity is associated with aggressive phenotypes, whereas in liver and kidney, G6PC loss promotes metabolic disruption and dedifferentiation. This Review highlights how ER-directed G6P flux, rather than glucose production itself, may shape tumour behaviour and reveal context-specific therapeutic vulnerabilities. Importantly, the clinical targeting of this system remains at an early, largely preclinical stage, and the therapeutic opportunities discussed here should be regarded as hypotheses to be tested rather than established interventions. - Source: PubMed
Publication date: 2026/07/17
Danalache Bogdan AlexandruFallah AbdallahMercier FrédéricAnnabi Borhane - SLC37A4 mediates glucose-6-phosphate transport for glucose homeostasis. Two recent studies in PLOS Biology report its structures and, together with other reports, illuminate the glucose-6-phosphate/phosphate exchange cycle and its inhibition mechanism. - Source: PubMed
Publication date: 2026/07/29
Qi Lin KevinShen ChengHattori Motoyuki - Glucose 6 phosphate (G6P) homeostasis is essential for maintaining blood glucose levels and coordinating anabolic and catabolic pathways. A key step in this process is the delivery of G6P into the endoplasmic reticulum (ER), where it is hydrolyzed by glucose 6 phosphatase to glucose and inorganic phosphate (Pi). This transport step is carried out by the ER carrier SLC37A4 (also known as the G6P transporter, G6PT), which imports G6P into the ER lumen while exporting Pi to the cytosol, and loss-of-function mutations in SLC37A4 cause glycogen storage disease type Ib. Despite its central role in G6P homeostasis, how SLC37A4 recognizes G6P and couples its transport to Pi antiport has remained unclear. Here we report cryo-electron microscopy structures of human SLC37A4 in three states: the apo form at 2.8 Å resolution, a G6P-bound state at 3.2 Å resolution and a chlorogenic acid (CHA) bound state at 3.3 Å resolution. SLC37A4 adopts the canonical Major Facilitator Superfamily fold and harbors a central, positively charged cavity that accommodates anionic substrates. In the G6P-bound structure, SLC37A4 adopts an outward-open conformation facing the ER lumen, in which G6P binds to the electropositive pocket. In the CHA-bound structure, SLC37A4 adopts an inward-facing conformation, with CHA bound at a cytosolic site that locks the transporter in an arrested state and prevents the conformational transitions required for G6P/Pi exchange. Combined with thermostability and transport-based analyses of G6P binding and disease variants, these structures support a rocker switch mechanism in which electrostatic neutralization of the central positively charged cavity by anionic substrate drives the conformational changes underlying G6P/Pi exchange. Together, these findings define the structural basis of G6P/Pi exchange by SLC37A4, provide a molecular rationale for pathogenic mutations in glycogen storage disease type Ib, and provide a framework for targeting SLC37A4 to modulate G6P homeostasis. - Source: PubMed
Publication date: 2026/07/28
Li HuiPeng XiaominHuang YuwenWu WenchengLi NanCheng ZiqiWei Xuepeng