High impact information on RANGAP1

• We have found that the mammalian Ran GTPase-activating protein RanGAP1 is highly concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it associates with the 358-kDa Ran-GTP-binding protein RanBP2 [1].
• However, injection of Ran GTPase-activating protein (RanGAP) into RCC1-depleted cell nuclei inhibited export [2].
• A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex [3].
• Inactive, GDP-locked RanT24N or nuclear microinjection of Ran GTPase activating protein 1 blocked Smad3 export [4].
• In addition, we demonstrated that SUMO-2/3 conjugated poorly, if at all, to a major SUMO-1 substrate, the Ran GTPase-activating protein RanGAP1 [5].

Biological context of RANGAP1

• We further showed that both sentrin-1 and sentrin-2 could covalently modify RanGAP1, a Ran GTPase-activating protein critically involved in nuclear transport [6].
• Interaction of karyopherin alpha and a classical nuclear localization sequence peptide with the Kapbeta1.RanGTP.RBH complex stimulated GTP hydrolysis by Ran GTPase activating protein 1 both in vitro and in permeabilized cells [7].

Associations of RANGAP1 with chemical compounds

• In vertebrates, these functions are controlled by a three-dimensional gradient of Ran-GTP to Ran-GDP, established by the spatial separation of Ran GTPase-activating protein (RanGAP) and the Ran guanine nucleotide exchange factor RCC1 [8].

Other interactions of RANGAP1

• RBH complex resisted dissociation by RanBP1 and GTP hydrolysis by Ran GTPase activating protein 1 [7].
• In addition the G19V Ran and effector domain mutants (L43E and E46G Ran) were not sensitive to the GTPase-activating protein, Fug1 [9].
• Modification of Ran GTPase-activating protein by the small ubiquitin-related modifier SUMO-1 requires Ubc9, an E2-type ubiquitin-conjugating enzyme homologue [10].
• Under the optimized condition, on-chip sumoylation of Ran GTPase-activating protein 1 (RanGAP1) domain resulted in highly specific fluorescence intensity compared to that of its mutant (K524A) irrelevant to SUMO conjugation [11].

Analytical, diagnostic and therapeutic context of RANGAP1

• Sequence analysis identified immunogenic antigens such as the cytochrome oxidase I, sp100 and Ran GTPase activating protein [12].

References