Snx1
- Known as:
- Snx1
- Catalog number:
- 060940A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Snx1
Related genes to: Snx1
- Gene:
- SNX1 NIH gene
- Name:
- sorting nexin 1
- Previous symbol:
- -
- Synonyms:
- SNX1A, MGC8664, HsT17379, Vps5
- Chromosome:
- 15q22.31
- Locus Type:
- gene with protein product
- Date approved:
- 1996-07-17
- Date modifiied:
- 2015-08-26
Related products to: Snx1
Related articles to: Snx1
- Retrograde transport is central to endomembrane homeostasis, yet the identity and origin of plant retrograde carriers remain unresolved. Prevailing models propose that plant vacuolar sorting receptors (VSRs) recycle either from multivesicular bodies (MVBs) to the trans-Golgi network (TGN) or from the TGN to the Golgi apparatus and/or endoplasmic reticulum (ER). However, the ultrastructural features of plant retrograde transport carriers remain largely unresolved. Here, we show that plant retrograde transport is likely mediated by a previously unrecognized class of MVB-derived spherical vesicles. Using correlative light and electron microscopy and three-dimensional electron tomography, we identify a distinct population of ~30-50 nm spherical vesicles adjacent to MVBs, including nascent vesicles budding from the MVB limiting membrane in Arabidopsis root cells. Immunogold labeling shows that these vesicles are enriched in retromer components and VSRs, suggesting that they possibly function as retrograde transport carriers. To investigate their biogenesis, we perform cryo-electron microscopy and liposome tubulation assays, showing that Arabidopsis SNX1 generates shorter membrane tubules than its mammalian counterpart, consistent with reduced membrane affinity linked to differences in the amphipathic helix. Notably, the SNX1-SNX2 heterodimer produces heterogeneous structures, including spherical vesicles, recapitulating in vivo observations. Lastly, knockdown of SNX1 or SNX2 results in vacuolar mislocalization and increased degradation of GFP-VSR2, and defects in SNX1 and VPS29 inhibit formation of spherical vesicles adjacent to MVBs, resulting in embryonic lethality before the globular stage. Together, these findings establish MVB-derived spherical vesicles as plant retrograde carriers and reveal a distinct SNX-mediated mechanism underlying their formation. - Source: PubMed
Publication date: 2026/03/24
Li YanbinTao RanZhang HaiWen XiaokangLeung Stephen King PongQi QingZheng XiaohuiGuo HaoxuanWu CongxianFu ZhifeiHuang XiaorongLau Wilson Chun YuJiang LiwenCui Yong - Phosphatase and tensin homolog (PTEN) is a critical regulator of cell proliferation, differentiation, and inflammatory balance. However, its downstream proteomic effects in periodontal ligament stem cells (PDLSCs) remain poorly understood. This study aimed to elucidate the proteomic alterations induced by PTEN inhibition and identify potential molecular pathways underlying periodontal regeneration. - Source: PubMed
Publication date: 2026/03/20
Phothichailert SuphalakNowwarote NunthawanKornsuthisopon ChatvadeeMurakami ShinyaSrithanyarat Supreda SuphanantachatOsathanon Thanaphum - Cellular membrane trafficking, including endocytosis and exocytosis, is a complex process coordinated by trafficking-associated proteins, cargo molecules, the cytoskeleton, and membrane lipids. The NIMA-related kinases NEKL-2 (human NEK8/9) and NEKL-3 (human NEK6/7) are conserved regulators of membrane trafficking in Caenorhabditis elegans that are required for the completion of molting. Using a genetic approach, we isolated reduction-of-function mutations in piki-1 that suppress nekl-associated molting defects. piki-1 encodes the sole predicted C. elegans Class II PI 3-kinase (PI3K), a relatively understudied class of lipid modifiers that contribute to the production of PI 3-phosphate (PI(3)P) and PI 3,4-bisphosphate (PI(3,4)P2). Using genetically encoded lipid sensors, we found that PIKI-1 was responsible for the production of PI(3,4)P2 in the C. elegans epidermis but played only a minor role in contributing to PI(3)P levels. Consistent with this, both PI(3,4)P2 and PIKI-1 partially colocalized to early endosomes, and reduction of PIKI-1 affected the size and protein composition of early endosomal compartments marked by RAB-5, EEA-1, and SNX-1. Reduced PIKI-1 also led to increased tubulation of endosomal compartments associated with recycling or the degradation of cellular debris. In contrast to studies using mammalian cell culture, PIKI-1 was largely dispensable for clathrin-mediated endocytosis in the worm epidermis, a polarized epithelium. Notably, reduction of PIKI-1 function mitigated defects in early endosomes associated with the depletion of NEKL-2. We propose that reduction of PIKI-1 function may suppress nekl molting defects by partially restoring endocytic trafficking function within a subset of compartments, including the early endosome. We also show that inhibition of HIPR-1, an ortholog of the mammalian PI(3,4)P₂-binding proteins, HIP1 and HIPR1, suppresses nekl molting defects, consistent with a model that loss of PIKI-1 alters the binding of endocytic regulators in a manner that partially compensates for the loss of NEKL-2 activity. - Source: PubMed
Publication date: 2026/02/13
Reimann Gabrielle REdeen Philip TConquest SylviaGrant Barth DFay David S - Sorting nexin 1 (SNX1), a member of the sorting nexin family, has been implicated in various cellular processes, yet its role in ovarian cancer (OV) remains poorly characterized. In this study, we systematically investigated the expression pattern, prognostic relevance and functional impact of SNX1 in OV. Bioinformatics analysis revealed that SNX1 is significantly downregulated in OV tissues, and its low expression is associated with poor overall and progression-free survival. Gene set enrichment analysis indicated that SNX1 downregulation is linked to activation of cancer-related pathways, including p53 signaling, PI3K/AKT signaling, and cell cycle-associated programs such as E2F targets and G2/M checkpoint. Functionally, SNX1 overexpression inhibited OV cell proliferation, blocked G1/S transition (with downregulation of E2F1, CDK2, CDK6, and cyclin D1), promoted apoptosis, and suppressed cell migration by modulating EMT markers (upregulating E-cadherin; downregulating -cadherin, vimentin, Snail1, and -catenin). Drug sensitivity analysis demonstrated a synergistic anti-tumor effect between SNX1 overexpression and paclitaxel treatment. Collectively, our findings identify SNX1 as a tumor suppressor and potential therapeutic target in OV, functioning through regulation of cell cycle, apoptosis and migration. - Source: PubMed
Publication date: 2025/12/31
Li PinYu XiaoyanWen KailingWang LeiYu JingranChen Ping - Despite technological advances, missing proteins remain a challenge in proteomics, obscuring proteins that are biologically or clinically important. We present Protrec2, a probabilistic framework that integrates tissue-specific protein complex annotations with Bayesian inference to recover unreported but biologically present proteins. We benchmarked Protrec2 on HeLa and A549-derived proteomes under "upper-bound" and "lower-bound" scenarios, reflecting distinct but complementary real-world use cases. In upper-bound evaluations, Protrec2 consistently outperformed state-of-the-art methods such as PROTein RECovery, Functional Class Scoring, Hypergeometric Enrichment, and Gene Set Enrichment Analysis, achieving the highest recovery rates: up to 98.4% in A549 and 96.5% in HeLa and validating 650 and 453 proteins, respectively. In lower-bound evaluations, Protrec2 maintained superior precision, validating over 90% of its predicted proteins in the A549 dataset and 74.6% in HeLa, while other methods exhibited significant performance drops. We applied Protrec2 to six matched lung tumor-normal pairs and validated predictions against CPTAC. Over 85% of predicted proteins were supported, with cancer-specific proteins mostly upregulated and normal-exclusive ones downregulated. Frequently recovered proteins (e.g. P4HA3, SNX1, HIP1R, NOS2) are known to play key roles in lung cancer, highlighting the biological and clinical relevance of Protrec2. These findings establish Protrec2 as a robust, biologically grounded tool for missing protein recovery, with broad applicability in discovery proteomics and translational research. - Source: PubMed
Kong WeijiaGoh Wilson Wen BinWong Limsoon