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Ran GTPase activating protein 1

RanGAP1, RanGAP, Segregation Distorter
RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. RanGAP1 is the immediate antagonist of RCC1, a regulator molecule that keeps RAN in the active, GTP-bound state. The RANGAP1 gene encodes a 587-amino acid polypeptide. The sequence is unrelated to that of GTPase activators for other RAS-related proteins, but is 88% identical to Fug1, the murine homolog of yeast Rna1p. RanGAP1 and RCC1 control RAN-dependent transport between the nucleus and cytoplasm. RanGAP1 is a key regulator of the RAN GTP/GDP cycle. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: RAN, Smt3, Ubiquitin, DAPI, CAN
Papers on RanGAP1
Evaluation of the activity and substrate specificity of the human SENP family of SUMO proteases.
Pinto et al., Porto, Portugal. In Biochim Biophys Acta, Jan 2016
ProSUMO1/2/3, RanGAP1-SUMO1/2/3 and polySUMO2/3 chains were used as substrates in these analyses.
Proteomics-Based Identification and Analysis of Proteins Associated with Helicobacter pylori in Gastric Cancer.
Guan et al., Guiyang, China. In Plos One, Dec 2015
We detected 135 differently expressed proteins from the three cell lines using proteome technology, and 10 differential proteins common to the three cell lines were selected and identified by LC-MS/MS as well as verified by western blot: β-actin, L-lactate dehydrogenase (LDH), dihydrolipoamide dehydrogenase (DLD), pre-mRNA-processing factor 19 homolog (PRPF19), ATP synthase, calmodulin (CaM), p64 CLCP, Ran-specific GTPase-activating protein (RanGAP), P43 and calreticulin.
The Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells.
Rudd et al., Cambridge, United Kingdom. In Mol Cell, Oct 2015
NPC has cytoplasmic filaments composed of RanGAP1 and RanBP2 with the potential to interact with cytoplasmic mediators.
The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.
Rothstein et al., United States. In Nature, Oct 2015
A candidate-based genetic screen in Drosophila expressing 30 G4C2 repeats identified RanGAP (Drosophila orthologue of human RanGAP1), a key regulator of nucleocytoplasmic transport, as a potent suppressor of neurodegeneration.
The Cellular Distribution of RanGAP1 Is Regulated by CRM1-Mediated Nuclear Export in Mammalian Cells.
Zhang et al., Detroit, United States. In Plos One, 2014
The Ran GTPase activating protein RanGAP1 plays an essential role in nuclear transport by stimulating RanGTP hydrolysis in the cytoplasmic compartment.
Molecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells.
Zhang et al., Detroit, United States. In Plos One, 2014
Here we show that SUMO1-modification of the Ran GTPase-activating protein RanGAP1 not only target RanGAP1 to its known sites at nuclear pore complexes but also to annulate lamellae pore complexes through interactions with the Ran-binding protein RanBP2 and the SUMO-conjugating enzyme Ubc9 in mammalian cells.
KASHing up with the nucleus: novel functional roles of KASH proteins at the cytoplasmic surface of the nucleus.
Starr et al., Minneapolis, United States. In Curr Opin Cell Biol, 2014
New findings have expanded the functional diversity of KASH proteins, showing that they interact with microtubule motors, actin, intermediate filaments, a nonconventional myosin, RanGAP, and each other.
The selfish Segregation Distorter gene complex of Drosophila melanogaster.
Presgraves et al., Rochester, United States. In Genetics, 2012
The Sd-RanGAP protein is enzymatically wild type but mislocalized within cells and, for reasons that remain unclear, appears to disrupt the histone-to-protamine transition in drive-sensitive spermatids bearing many Rsp satellite repeats but not drive-insensitive spermatids bearing few or no Rsp satellite repeats.
Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2.
Lima et al., New York City, United States. In J Biol Chem, 2012
Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2.
Physical breakdown of the nuclear envelope is not necessary for breaking its barrier function.
Haraguchi et al., Suita, Japan. In Nucleus, 2011
The key event in V-NEBD is nuclear translocation of Rna1, a RanGAP1 homologue in S. pombe.
RanGAP is required for post-meiotic mitosis in female gametophyte development in Arabidopsis thaliana.
Meier et al., Columbus, United States. In J Exp Bot, 2011
These results show that the two RanGAPs are redundant and indispensable for female gametophyte development in Arabidopsis but dispensable for pollen development.
Alternative allosteric mechanisms can regulate the substrate and E2 in SUMO conjugation.
Haliloğlu et al., İstanbul, Turkey. In J Mol Biol, 2011
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.
The protein composition of mitotic chromosomes determined using multiclassifier combinatorial proteomics.
Rappsilber et al., Edinburgh, United Kingdom. In Cell, 2010
An unbiased analysis of the whole chromosome proteome from genetic knockouts of kinetochore protein Ska3/Rama1 revealed that the APC/C and RanBP2/RanGAP1 complexes depend on the Ska complex for stable association with chromosomes.
Targeting proteins to the plant nuclear envelope.
Xu et al., Columbus, United States. In Biochem Soc Trans, 2010
We are using the case of the nuclear pore-associated Ran-cycle component RanGAP (Ran GTPase-activating protein) to address these fundamental questions.
WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1.
Meier et al., Columbus, United States. In Plant Physiol, 2009
These data suggest that both HSC70-1 and the WPP-domain proteins play a role in facilitating WIT1 nuclear envelope targeting; this may be the first described in planta activity for the WPP-domain proteins.
Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1.
Matunis et al., Baltimore, United States. In Mol Cell, 2009
Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1.
An in vitro FRET-based assay for the analysis of SUMO conjugation and isopeptidase cleavage.
Melchior et al., Göttingen, Germany. In Methods Mol Biol, 2008
The assay described here uses bacterially expressed and purified YFP-SUMO-1 and CFP-RanGAP1 as model substrates that are covalently coupled in the presence of recombinant SUMO E1 and E2 enzymes and ATP.
Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.
Lima et al., New York City, United States. In Nature, 2005
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
Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.
Lima et al., New York City, United States. In Cell, 2002
Crystallographic analysis of a complex between mammalian Ubc9 and a C-terminal domain of RanGAP1 at 2.5 A reveals structural determinants for recognition of consensus SUMO modification sequences found within SUMO-conjugated proteins.
RanGAP mediates GTP hydrolysis without an arginine finger.
Vetter et al., Dortmund, Germany. In Nature, 2002
Ran-GTP is hydrolysed by the combined action of Ran-binding proteins (RanBPs) and RanGAP.
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