Ask about this productRelated genes to: Sh3gl3 antibody
- Gene:
- SH3GL3 NIH gene
- Name:
- SH3 domain containing GRB2 like 3, endophilin A3
- Previous symbol:
- -
- Synonyms:
- SH3D2C, SH3P13, CNSA3, EEN-B2, HsT19371
- Chromosome:
- 15q25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1996-10-26
- Date modifiied:
- 2016-10-05
Related products to: Sh3gl3 antibody
Related articles to: Sh3gl3 antibody
- The endophilin protein family comprises a group of evolutionarily highly conserved Bin-Amphiphysin-Rvs (BAR) domain proteins that play key roles in cell membrane morphogenesis, endocytic trafficking, and organelle dynamics. The human endophilin family includes five main members, encoded by the genes (endophilin A1), (endophilin A2), (endophilin A3), (endophilin B1), and (endophilin B2). Notably, gives rise to functionally distinct splice variants, including the ubiquitously expressed B1a and the neuron-enriched B1b/c, which play critical, opposing roles in conditions such as Alzheimer disease (AD). These isoforms perform distinct, often opposing functions in disease pathogenesis via specific molecular mechanisms. For instance, endophilin A1 acts as a tumor suppressor; its gene, , is frequently deleted or downregulated in cancers such as non-small cell lung cancer, and its loss promotes tumor progression by sustaining epidermal growth factor receptor (EGFR) signaling. Conversely, endophilin A2 drives cancer metastasis. In AD, endophilin A1 expression is significantly elevated, exacerbating synaptic dysfunction, while neuron-specific endophilin B1 isoforms are decreased, worsening amyloid pathology. The regulation of endophilins involves intricate networks, including post-transcriptional control by microRNAs (e.g., miR-330 targeting in glioblastoma) and post-translational modifications. This review provides a comprehensive overview of the structural characteristics and regulation of expression and activity. It delineates the molecular mechanisms by which their dysfunction contributes to disease pathogenesis, aiming to provide new insights into these multifaceted proteins in health and disease. - Source: PubMed
Liu XiaoyunFan ShuxianPan XuediaoPang HuiminSu WenweiLiu Song - - Source: PubMed
Publication date: 2026/08/04
Yueqing WangLei XuXu WangJiao WangLimin GuZhongbo Shang - Insight into the conformational dynamics of proteins is essential toward understanding their function at a molecular level. The motions experienced by individual atoms in the protein can be precisely quantified through NMR relaxation rates, but their measurement requires well-resolved spectral responses. Two-dimensional H-N correlation spectra are the standard approach to resolve amide signals in protein NMR, but come with an excessive cost in experimental time when spectra are heavily congested due to limited N chemical shift dispersions. This limitation often thwarts the characterization of dynamics for intrinsically disordered proteins, especially when they feature low-complexity or homopolymer regions, or short sample life-times. Here, we introduce a fast, ultra-selective H-N 1D NMR method that allows high-quality measurement of individual N spin-relaxation constants, even when N resonances are merely 6-8 Hz apart. We demonstrate the new experiment by characterizing, for the first time, pico- to nanosecond dynamics along a 16-residue polyglutamine stretch within the protein huntingtin, the causal agent of Huntington's disease, as well as millisecond conformational exchange in the SH3GL3 protein. The new experiment will find wide application in the study of conformational dynamics of intrinsically disordered proteins or any other biomacromolecule that features highly dense H-N 2D spectra. - Source: PubMed
Publication date: 2026/02/17
Adamski WiktorLevy Geraldine RCantrelle François-XavierSinnaeve Davy - Ambient air pollution contributes to chronic obstructive pulmonary disease (COPD), but the genetic factors that may influence susceptibility remain poorly defined. We conducted a genome-wide interaction analysis to identify genetic markers that may modify the association between air pollution and COPD. We analyzed data from 16,839 Canadian Longitudinal Study of Aging participants, including spirometry, genome-wide genotype data (645,625 single-nucleotide polymorphisms [SNPs]), and air pollution exposure estimates. COPD was defined as a forced expiratory volume in 1 second to forced vital capacity ratio (FEV/FVC) below the lower limit of normal. Annual average concentrations of particulate matter (PM), nitrogen dioxide (NO), and ozone (O), representing multi-year exposure estimates (2012-2015), were assigned to participants' residential postal code. Logistic regression models with SNP-by-air-pollutant interaction terms were applied, with a significant interaction threshold set at p < 7.74 × 10 after Bonferroni correction. Significant interactions were observed between PM and rs3762953 in CEP72/TPPP (P = 4.82 × 10) and rs72802672 in WFDC1 (P5.62 × 10). For NO, significant interactions were observed with rs2585043 near ADAMTSL3/SH3GL3 (P4.01 × 10), rs6809120 in ADAMTS9 (P4.53 × 10), rs6761941 near EPCAM-DT/CALM2 (P5.12 × 10), rs113083358 in DLG2 (P6.44 × 10), and rs17801230 near FASTKD2/CPO (P4.69 × 10). These loci map to genes involved in microtubule and ciliary function, extracellular matrix remodeling and protease regulation, airway inflammation and smooth muscle contractility, and mitochondrial function. These findings highlight genetic modification of the association between air pollution and COPD susceptibility in low-exposure settings and offer mechanistic insight without implying direct clinical application. - Source: PubMed
Publication date: 2026/01/20
Odimba UgochukwuFarrell JamieSadatsafavi MohsenJiang XiantaGao Zhiwei - Endophilin A, a family of Bin-Amphoterisin-Rvs (BAR) domain-conserved proteins, is found in several tissues and is associated with disease pathogenesis. In patients with breast cancer, endophilin A expression pertains to boosted tumour cell endocytosis, migration, and invadopodia formation, potentially linked to a poor prognosis. - Source: PubMed
Publication date: 2025/10/08
Mehta VikrantIslam SohidulKasana HaritChander Harish