RANBP2

RANBP2

A gene on chromosome 2q12.3 that encodes a very large RAN-binding protein that immunolocalises to the nuclear pore complex. It is a scaffold and mosaic cyclophilin-related nucleoporin involved in the Ran-GTPase cycle; it interacts directly with the E2 enzyme UBC9 and enhances the transfer of SUMO1 (sumoylation) to its target SP100. RANBP2 is partially duplicated in a gene cluster that lies in the chromosome 2 recombination hot spot.
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In extrauterine IMTs, patterns of immunostaining have been correlated with specific gene fusions depending on the location of the fusion partner such as nuclear membrane staining with RANBP2-ALK fusion, since RANBP2 is a nuclear pore protein.
Cytoplasmic filaments are predominantly composed of Nup88, Nup214 (CAN), and Nup358 (RanBP2), whereas the main constituents of the nuclear basket are Tpr, Nup153, and Npap60 (Nup50).
On the other hand, although Ran has its own weak hydrolytic activity, the hydrolysis of RanGTP to RanGDP is strongly accelerated by the GTPase-activating protein RanGAP1, in conjunction with Ran binding protein 1 (RanBP1) and/or Ran binding protein 2 (RanBP2, also called Nup358).
Starting from the array-CGH results, eight forward primers (LIMS1_F1-8) were designed in the 42 kb interval between the normal dosage probe and the deleted probe in LIMS1 (chr2:109258450-109300532) and five reverse primers (RANBP2_R1-5) were designed in the 24 kb interval between the deleted probe and the normal dosage probe in RANBP2 (chr2:109380702-109405259).
Senda et al., "Selective impairment of a subset of Ran-GTP-binding domains of Ran-binding protein 2 (Ranbp2) suffices to recapitulate the degeneration of the retinal pigment epithelium (RPE) triggered by Ranbp2 ablation," The Journal of Biological Chemistry, vol.
Ferreira, "Ranbp2 haploinsufficiency mediates distinct cellular and biochemical phenotypes in brain and retinal dopaminergic and glia cells elicited by the Parkinsonian neurotoxin, 1-methyl-4-phenyl1,2,3,6-tetrahydropyridine (MPTP)," Cellular and Molecular Life Sciences, vol.
Familial or recurrent cases of infection-triggered acute necrotizing encephalopathy can be caused by a RANBP2 gene mutation [18].
Various novel proteins have also been shown to be direct substrates of p38[alpha], including Ahnak, Iws1, Grp78, Pgrmc, Prdx6, and Ranbp2 [71].
Mutation in the gene Ran-binding 2 (RANBP2) have been shown to be associated with familial or recurrent influenza-associated acute encephalopathy/encephalitis (23).
(8,15) Several ALK fusion partners have been identified, including TPM3, TPM4, CLTC, RANBP2, and ATIC.
The ALK gene rearrangements identified that have led to fusion with other genes include ATIC, (41) CARS, (61,62) TPM3, (63-65) TPM4, (63,65,66) TPM3 and TPM4, (67) CLTC, (60,65,68) RANBP2, (60,69) and SEC31L1 (SEC31A).
(194) Inflammatory myofibroblastic tumors express ALK fusions with tropomyosin genes TPM3 and TPM4, CLTC, ATIC, and less frequently, RANBP2 (RAN-binding protein 2), CARS (cysteinyl-tRNA synthetase), and SEC31A (SEC-like 1) that are not expressed in ALCL.