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RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. Additionally we are shipping Ran GTPase Activating Protein 1 Antibodies (85) and Ran GTPase Activating Protein 1 Proteins (5) and many more products for this protein.
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our results elucidate that RanGAP1 is actively transported between the nuclear and cytoplasmic compartments, and that the cytoplasmic and NPC (show NPC1 ELISA Kits) localization of RanGAP1 is dependent on CRM1 (show XPO1 ELISA Kits)-mediated nuclear export.
immune cell adaptor SLP-76 (show LCP2 ELISA Kits) binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits) p65 (show GORASP1 ELISA Kits) nuclear entry in T cells
Differentiation of human coronary artery smooth muscle cell to a contractile phenotype by stepwise serum depletion leads to significant reduction of RanGAP1 protein levels.
Determinants of small ubiquitin-like modifier 1 (SUMO1 (show SUMO1 ELISA Kits)) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin (show AGFG2 ELISA Kits) RanBP2 (show RANBP2 ELISA Kits).
Analysis of the dynamics of E2(Ubc9 (show UBE2I ELISA Kits))-SUMO-Target(RanGAP1) in the absence and presence of E3(RanBP2 (show RANBP2 ELISA Kits)) revealed that two different allosteric sites regulate the ligase activity.
the RanGAP1 consensus sumoylation site and SUMO-1 (show SUMO1 ELISA Kits) C terminus are both conformationally flexible
the 3.0-A crystal structure of a four-protein complex of Ubc9 (show UBE2I ELISA Kits), a Nup358/RanBP2 (show RANBP2 ELISA Kits) E3 ligase domain (IR1 (show NISCH ELISA Kits)-M) and SUMO-1 (show SUMO1 ELISA Kits) conjugated to the carboxy-terminal domain of RanGAP1
RanGAP1 is phosphorylated on Ser (show SIGLEC1 ELISA Kits)-358 in vivo & in vitro. Phosphorylated RanGAP1, but not a mutant at 358S, formed a stable ternary complex with Ran and RanBP1 (show RANBP1 ELISA Kits) in vivo, suggesting that its 358S phosphorylation affects the Ran system.
The results of this study strengthen the conclusion that mel-18 (show PCGF2 ELISA Kits) functions as an anti-SUMO E3 factor, and extend its targets to include regulation of the sumoylation of the important cellular protein RanGAP1.
nuclear localization of Ran was strongly increased in MYCBP2-deficient DRGs
immune cell adaptor SLP-76 (show LCP2 ELISA Kits) binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits) p65 (show NFkBP65 ELISA Kits) nuclear entry in T cells
These data suggest a dual function of the Nup358 (show RANBP2 ELISA Kits)-RanGAP1 complex as a coordinator of importin beta (show KPNB1 ELISA Kits) recycling and reformation of novel import complexes.
Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1.
The data show that plant development is differentially affected by RanGAP mutant allele combinations of increasing severity and requires the GAP activity of RanGAP, while the subcellular positioning of RanGAP is dispensable.
AtRanGAP1 has a mitotic trafficking pattern uniquely different from that of vertebrate RanGAP.
In a wip1-1/wip2-1/wip3-1 triple mutant, RanGAP1 is dislocated from the nuclear envelope in undifferentiated root-tip cells, whereas nuclear envelope targeting in differentiated root cells and targeting to the cell plate remain intact.
Data suggest that an unanticipated complexity of RanGAP nuclear envelope targeting and at least one member of each NE-associated coiled-coil and transmembrane domains protein family is required for RanGAP targeting in root tip cells.
propose that Arabidopsis RanGAP, a continuous positive protein marker of the plant division plane, has a role in spatial signaling during plant cell division
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.
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.
ran GTPase-activating protein 1
, ran GTPase activating protein 1
, Ran GTPase activating protein 1
, Ran GTPase activating protein 1 b
, segregation distorter homolog
, segregation distortion
, RAN GTPase activating protein 1
, RAN GTPase activating protein 1 a