| Hepatitis B virus core protein stabilizes RANGAP1 to upregulate KDM2A and facilitate hepatocarcinogenesis. | Hepatitis B virus core protein stabilizes RANGAP1 to upregulate KDM2A and facilitate hepatocarcinogenesis.
You HJ, Ma LH, Wang X, Wang YX, Zhang HY, Bao ES, Zhong YJ, Liu XY, Kong DL, Zheng KY, Kong FY, Tang RX. | 06/11/2024 |
| SUMOylation mediates the disassembly of the Smad4 nuclear export complex via RanGAP1 in KELOIDS. | SUMOylation mediates the disassembly of the Smad4 nuclear export complex via RanGAP1 in KELOIDS.
Lin X, Pang Q, Hu J, Sun J, Dai S, Yu Y, Xu J., Free PMC Article | 04/19/2023 |
| Loss of RanGAP1 drives chromosome instability and rapid tumorigenesis of osteosarcoma. | Loss of RanGAP1 drives chromosome instability and rapid tumorigenesis of osteosarcoma.
Gong Y, Zou S, Deng D, Wang L, Hu H, Qiu Z, Wei T, Yang P, Zhou J, Zhang Y, Zhu W, Xie X, Liao Z, Yang J, Zhang S, Liu A, Jiang Y, Zou Z, Bai X. | 02/12/2023 |
| CircRNA_0079586 and circRNA_RanGAP1 are involved in the pathogenesis of intracranial aneurysms rupture by regulating the expression of MPO. | CircRNA_0079586 and circRNA_RanGAP1 are involved in the pathogenesis of intracranial aneurysms rupture by regulating the expression of MPO.
Zhang Z, Sui R, Ge L, Xia D., Free PMC Article | 01/1/2022 |
| The RanBP2/RanGAP1-SUMO complex gates beta-arrestin2 nuclear entry to regulate the Mdm2-p53 signaling axis. | The RanBP2/RanGAP1-SUMO complex gates β-arrestin2 nuclear entry to regulate the Mdm2-p53 signaling axis.
Blondel-Tepaz E, Leverve M, Sokrat B, Paradis JS, Kosic M, Saha K, Auffray C, Lima-Fernandes E, Zamborlini A, Poupon A, Gaboury L, Findlay J, Baillie GS, Enslen H, Bouvier M, Angers S, Marullo S, Scott MGH. | 10/16/2021 |
| Circular RNA circ-RanGAP1 regulates VEGFA expression by targeting miR-877-3p to facilitate gastric cancer invasion and metastasis. | Circular RNA circ-RanGAP1 regulates VEGFA expression by targeting miR-877-3p to facilitate gastric cancer invasion and metastasis.
Lu J, Wang YH, Yoon C, Huang XY, Xu Y, Xie JW, Wang JB, Lin JX, Chen QY, Cao LL, Zheng CH, Li P, Huang CM. | 08/29/2020 |
| NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division. | Nucleolar and spindle-associated protein 1 (NUSAP1) interacts with a SUMO E3 ligase complex during chromosome segregation.
Mills CA, Suzuki A, Arceci A, Mo JY, Duncan A, Salmon ED, Emanuele MJ., Free PMC Article | 10/28/2017 |
| RanGAP1 upregulation is associated with drug resistance in Chronic Myeloid Leukemia. | MicroRNA-1301-Mediated RanGAP1 Downregulation Induces BCR-ABL Nuclear Entrapment to Enhance Imatinib Efficacy in Chronic Myeloid Leukemia Cells.
Lin TY, Chen KC, Liu HJ, Liu AJ, Wang KL, Shih CM., Free PMC Article | 08/5/2017 |
| Abnormal localization of RanGAP1 was found in cortex of Huntington's disease patients. | Polyglutamine-Expanded Huntingtin Exacerbates Age-Related Disruption of Nuclear Integrity and Nucleocytoplasmic Transport.
Gasset-Rosa F, Chillon-Marinas C, Goginashvili A, Atwal RS, Artates JW, Tabet R, Wheeler VC, Bang AG, Cleveland DW, Lagier-Tourenne C., Free PMC Article | 07/29/2017 |
| our results elucidate that RanGAP1 is actively transported between the nuclear and cytoplasmic compartments, and that the cytoplasmic and NPC localization of RanGAP1 is dependent on CRM1-mediated nuclear export. | The Cellular Distribution of RanGAP1 Is Regulated by CRM1-Mediated Nuclear Export in Mammalian Cells.
Cha K, Sen P, Raghunayakula S, Zhang XD., Free PMC Article | 06/11/2016 |
| immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 and NF-kappaB p65 nuclear entry in T cells | The Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells.
Liu H, Schneider H, Recino A, Richardson C, Goldberg MW, Rudd CE., Free PMC Article | 11/28/2015 |
| Differentiation of human coronary artery smooth muscle cell to a contractile phenotype by stepwise serum depletion leads to significant reduction of RanGAP1 protein levels. | The Ran GTPase-activating protein (RanGAP1) is critically involved in smooth muscle cell differentiation, proliferation and migration following vascular injury: implications for neointima formation and restenosis.
Vorpahl M, Schönhofer-Merl S, Michaelis C, Flotho A, Melchior F, Wessely R., Free PMC Article | 10/24/2015 |
| Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2. | Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2.
Gareau JR, Reverter D, Lima CD., Free PMC Article | 04/21/2012 |
| Analysis of the dynamics of E2(Ubc9)-SUMO-Target(RanGAP1) in the absence and presence of E3(RanBP2) revealed that two different allosteric sites regulate the ligase activity. | Alternative allosteric mechanisms can regulate the substrate and E2 in SUMO conjugation.
Karaca E, Tozluoğlu M, Nussinov R, Haliloğlu T., Free PMC Article | 04/9/2011 |
| The results of this study strengthen the conclusion that mel-18 functions as an anti-SUMO E3 factor, and extend its targets to include regulation of the sumoylation of the important cellular protein RanGAP1. | Mel-18 interacts with RanGAP1 and inhibits its sumoylation.
Zhang J, Sarge KD., Free PMC Article | 01/21/2010 |
| the 3.0-A crystal structure of a four-protein complex of Ubc9, a Nup358/RanBP2 E3 ligase domain (IR1-M) and SUMO-1 conjugated to the carboxy-terminal domain of RanGAP1 | Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.
Reverter D, Lima CD., Free PMC Article | 01/21/2010 |
| RanGAP1 is phosphorylated on Ser-358 in vivo & in vitro. Phosphorylated RanGAP1, but not a mutant at 358S, formed a stable ternary complex with Ran and RanBP1 in vivo, suggesting that its 358S phosphorylation affects the Ran system. | Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1.
Takeda E, Hieda M, Katahira J, Yoneda Y. | 01/21/2010 |
| the RanGAP1 consensus sumoylation site and SUMO-1 C terminus are both conformationally flexible | Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1.
Macauley MS, Errington WJ, Okon M, Schärpf M, Mackereth CD, Schulman BA, McIntosh LP. | 01/21/2010 |