Ask about this productRelated genes to: TNPO3 antibody
- Gene:
- TNPO3 NIH gene
- Name:
- transportin 3
- Previous symbol:
- LGMD1F
- Synonyms:
- TRN-SR, MTR10A, TRN-SR2, IPO12
- Chromosome:
- 7q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-09
- Date modifiied:
- 2016-10-05
Related products to: TNPO3 antibody
Related articles to: TNPO3 antibody
- Nuclear transport is a vital system that mediates movement of essential biomolecules between the nucleus and cytoplasm. It is tightly regulated by the Importin (IMP) superfamily to maintain separation of cellular compartments. Cellular stress in various forms, particularly oxidative, can suspend nuclear transport and lead to cell death. Prolonged oxidative stress manifests in myriad conditions, including cancer, viral infection and metabolic disease. An IMP protein, Importin-13 (IMP13), retains function under stress, while all other IMP family members tested to date do not. Phylogenetic and structural analysis revealed Transportin-3 (TNPO3) as the closest homologue of IMP13, suggesting it may also retain its function under stress. Subcellular localisation studies indicated that TNPO3 maintained its typical subcellular localisation, even in the presence of stress, unlike most IMP family members. Also, fluorescence recovery after photobleaching (FRAP) demonstrated that TNPO3 shuttling is unaffected under stress. Co-immunoprecipitation studies examining cargo binding revealed the capacity of TNPO3 to bind its cargo in the presence of stress. This demonstrated for the first time that TNPO3 retains functionality under stress conditions, in contrast to other IMPs, but similar to IMP13. Furthermore, both IMP13 and TNPO3 appear to protect against the potentially critical mislocalisation of Ran, a key molecule involved in the maintenance of the nuclear transport system. - Source: PubMed
Publication date: 2026/04/17
Barling Megan A LThomas David RJans David AWagstaff Kylie M - The past decade has seen remarkable progress in identifying genes that, when impacted by deleterious coding variation, confer high likelihood for autism spectrum disorder (ASD), intellectual disability and other associated developmental disorders. However, most underlying gene discovery efforts have focused on individuals of European ancestry, limiting insights into genetic liability across diverse populations. To help address this, the Genomics of Autism in Latin American Ancestries (GALA) Consortium was formed, presenting here the largest sequencing study of autism in Latin American individuals (n > 15,000, including 4,717 participants with an ASD diagnosis). We identified 35 genome-wide significant (false discovery rate < 0.05) autism-associated genes, with substantial overlap with findings from European cohorts, and highly constrained genes showing consistent signal across populations. The results provide support for emerging (for example, MARK2, YWHAG, PACS1, RERE, SPEN, GSE1, GLS, TNPO3 and ANKRD17) and established autism genes and for the utility of genetic testing approaches for deleterious variants in individuals from diverse backgrounds; the results also demonstrate the ongoing need for more inclusive genetic research and testing. We conclude that the biology of autism is consistent across populations, with no detectable influence of ancestry. - Source: PubMed
Publication date: 2026/03/30
Natividad Avila MarinaJung SeulgiSatterstrom F KyleFu Jack MLevy TessSloofman Laura GKlei LambertusPichardo TharianaMarquez DaliaStevens Christine RCusick Caroline MAmes Jennifer LCampos Gabriele SCerros HildaChaskel RobertoCosta Claudia I SCuccaro Michael LLopez Andrea Del PilarFernandez MagdalenaFerro EugenioGaleano LilianaGirardi Ana Cristina D E SGriswold Anthony JHernandez Luis CLourenço NailaLudena YuninNúñez-Ríos DianaOyama RosaPeña Katherine PPessah IsaacSchmidt RebeccaSweeney Holly MTolentino LizbethWang Jaqueline Y TAlbores-Gallo LiliaCroen Lisa ACruz-Fuentes Carlos SHertz-Picciotto IrvaKolevzon AlexanderLattig Maria ClaudiaMayo LilianaPassos-Bueno Maria RitaPericak-Vance Margaret ASiper Paige MTassone FloraTrelles M Pilar Talkowski Michael EDaly Mark JMahjani BehrangDe Rubeis SilviaCook Edwin HRoeder KathrynBetancur CatalinaDevlin BernieBuxbaum Joseph D - Nucleocytoplasmic transport relies on targeting signals within cargo polypeptides, typically as short linear motifs but sometimes as folded domains. These signals are recognized by the Karyopherin-β (Kap) family of importins, exportins, and biportins. Despite the number of Kaps, only a few linear signal classes are well-defined: the classical nuclear localization signal (cNLS) recognized by importin-α (IMPα), which in turn binds IMPβ to form the IMPα/β heterodimer, the IMPβ-binding domain, the Pro-Tyr NLS of transportin-1 (TNPO1/Kapβ2), the IK-NLS of Kap121/importin-5, and the RS/E- and RSY-NLSs of TNPO3, along with the classical nuclear export signal (NES) of exportin-1 (XPO1/CRM1) and the phosphorylated NES of yeast Msn5. This review summarizes recent structural and biochemical advances that define these signals and their recognition rules and highlights the remaining gaps in our understanding of linear signals across the Kap family. - Source: PubMed
Publication date: 2026/03/12
Wing Casey EChook Yuh Min - Transportin 3 (TNPO3) is a nuclear carrier for serine/arginine-rich proteins which are essential for mRNA splicing and metabolism. Mutations in the TNPO3 gene result in a protein with an extended C-terminal domain, leading to the onset of LGMDD2, a rare form of limb girdle muscular dystrophy. To investigate the role of TNPO3 in skeletal muscle and the pathogenic mechanism underlying LGMDD2, we develped both in vitro and in vivo models of the disease. The in vitro model was established using the C2C12 cell line, transfected with plasmids encoding either the wild-type (WT) or mutated (MUT) human TNPO3 (hTNPO3). For the in vivo model, we microinjected zebrafish (Danio rerio) embryos with mRNAs encoding WT or MUT hTNPO3. We analyzed the expression patterns of myogenesis-related genes, muscle-specific genes, myomiRNA and genes strictly related to the disease. These analyses were complemented by protein expression studies, morphological assessments in both models, and behavioral assays to validate the LGMDD2 zebrafish model. Our results demonstrate a key role for TNPO3 in regulating myogenesis in both models and reveal that the TNPO3 mutation disrupts normal myogenic commitment, supporting its contribution to LGMDD2 pathogenesis. Overall, this study represents a significant advance in understanding the role of TNPO3 in skeletal muscle biology and the molecular basis of LGMDD2. - Source: PubMed
Publication date: 2025/11/26
Rodia M TFazzina MCosta RobertaAltieri M TSabbioni GD'Aversa EBreveglieri GGatto EBertolucci CLombardi SBergonzoni MCasadei RSanti SPapa VRatti SCenacchi GBorgatti MFrabetti F - - Source: PubMed
Publication date: 2025/09/08
Kornienko JuliaSchraft LauraFenzl Kaivan den Hoogenhof Maarten M GSteinmetz Lars M