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These results demonstrate a function of RanBP2-mediated SUMOylation of SHP in maintaining bile acids (BA) homoeostasis and protecting from the BA hepatotoxicity.
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results demonstrate that Ranbp2 controls nucleocytoplasmic, chemokine and metalloproteinase 28 signaling, and proteostasis of substrates that are crucial to motoneuronal homeostasis and whose impairments by loss of Ranbp2 drive ALS-like syndromes
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RanBP2 expression was regulated by Zap70.
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Data (including data from studies in transgenic/knockout mice) suggest that Ranbp2 in photoreceptor neurons participates in coupling of photoreceptor degeneration (neural dysmorphology) and apoptosis (neural death) caused by toxic exposure to light.
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These studies unravel selective roles of Ranbp2 and its RBD2 and RBD3 in retinal pigment epithelium survival and functions.
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These results unveil distinct mechanistic and biological links between prolyl isomerase and chaperone activities of Ranbp2 cyclophilin toward proteostasis.
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Novel roles in Ran GTPase-independent subdomains of RBD2 and RBD3, and KBD of RanBP2, confer antagonizing and multi-modal mechanisms of kinesin-1 activation and regulation of mitochondrial motility.
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Ranbp2 haploinsufficiency is associated with metabolic imbalances leading to parkinson's disease.
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Knockdown of RANBP2 specifically affected the late step of nuclear entry, inducing cytoplasmic granules enriched with phosphorylated components. This suggests a novel regulatory mechanism for nuclear speckle formation involving RANBP2 and phosphorylation.
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A critical function of RanBP2 is to capture recycling RanGTP-importin-beta complexes at cytoplasmic fibrils to allow for adequate classical nuclear localization signal-mediated cargo import.
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findings indicate that the nuclear pore complex undergoes dynamic remodeling during muscle cell differentiation and that Nup358 is prominently involved in the remodeling process
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These results provide a rationale for the neuroprotection from light damage of photosensory neurons by RANBP2 insufficiency.
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RanBP2 associates in vitro and in vivo and colocalizes with the mitochondrial metallochaperone, Cox11, and the pacemaker of glycolysis, hexokinase type I (HKI) via its leucine-rich domain.
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binding of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function
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these data identify RanBP2 as a chromosomal instability gene that regulates Topo IIalpha by sumoylation and suppresses tumorigenesis.
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The RAN binding protein 2-dependent production of free fatty acids or metabolites promote apoptosis of photoreceptors in concert with the light-stimulated production of reactive oxygen species.
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reports identification of the cyclophilin-related protein, RanBP2 (note at the time the protein was not designated RanBP2), and the cis-trans prolyl isomerase activity of its cyclophilin domain
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reports interaction of the RBD4 and CY domains of RanBP2 with red/green opsin and the chaperone activity of these domains toward red/green opsin.
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reports interaction of the RBD4 and CY domains of RanBP2 with red/green opsin and the chaperone activity of these domains toward red/green opsin.
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reports identification of a binding domain in RanBP2, the cyclophilin-like domain, toward components of the 19S cap of the proteasome
