Two Putative Cypovirus-Encoded miRNAs Co-regulate the Host Gene of GTP-Binding Nuclear Protein Ran and Facilitate Virus Replication [PDF]
Frontiers in Physiology, 2021 microRNA (miRNA) plays important roles in regulating various biological processes, including host-pathogen interaction. Recent studies have demonstrated that virus-encoded miRNAs can manipulate host gene expression to ensure viral effective ...
Su Lin +19 more
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Kinesin-1 and mitochondrial motility control by discrimination of structurally equivalent but distinct subdomains in Ran-GTP-binding domains of Ran-binding protein 2 [PDF]
Open Biology, 2013 The pleckstrin homology (PH) domain is a versatile fold that mediates a variety of protein–protein and protein–phosphatidylinositol lipid interactions. The Ran-binding protein 2 (RanBP2) contains four interspersed Ran GTPase-binding domains (RBDn = 1–4 ...
Hemangi Patil +5 more
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Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. [PDF]
The EMBO Journal, 1995 RCC1 (the regulator of chromosome condensation) stimulates guanine nucleotide dissociation on the Ras-related nuclear protein Ran. Both polypeptides are components of a regulatory pathway that has been implicated in regulating DNA replication, onset of and exit from mitosis, mRNA processing and transport, and import of proteins into the nucleus.
F. Ralf Bischoff +4 more
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Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis. [PDF]
The Journal of cell biology, 1993 Ran/TC4, first identified as a well-conserved gene distantly related to H-RAS, encodes a protein which has recently been shown in yeast and mammalian systems to interact with RCC1, a protein whose function is required for the normal coupling of the completion of DNA synthesis and the initiation of mitosis.
Meng Ren +3 more
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Yrb4p, a yeast Ran-GTP-binding protein involved in import of ribosomal protein L25 into the nucleus [PDF]
The EMBO Journal, 1997 Gsp1p, the essential yeast Ran homologue, is a key regulator of transport across the nuclear pore complex (NPC). We report the identification of Yrb4p, a novel Gsp1p binding protein. The 123 kDa protein was isolated from Saccharomyces cerevisiae cells and found to be related to importin-beta, the mediator of nuclear localization signal (NLS)-dependent ...
Gabriel Schlenstedt
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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 [PDF]
Journal of Biological Chemistry, 2014 Retinal pigment epithelium (RPE) degeneration underpins diseases triggered by disparate genetic lesions, noxious insults, or both. The pleiotropic Ranbp2 controls the expression of intrinsic and extrinsic pathological stressors impinging on cellular viability. However, the physiological targets and mechanisms controlled by Ranbp2 in tissue homeostasis,
Hemangi Patil +10 more
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Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation [PDF]
Proceedings of the National Academy of Sciences, 2015 Significance The small GTPase Ran plays fundamental roles in cellular processes such as nucleo-cytoplasmic transport, mitotic spindle formation, and nuclear envelope assembly. Recently, Ran was found to be lysine acetylated, among others, in functionally important regions such as switch I and switch II.
Susanne de Boor +9 more
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Phenotype of the fission yeast cell cycle regulatory mutant pim1‐46 is suppressed by a tobacco cDNA encoding a small, Ran‐like GTP‐binding protein [PDF]
The Plant Journal, 1994 Mutations in which the onset of mitosis is uncoupled from the completion of DNA replication has recently been described. Characterization of these mutants led to the identification of Pim1/Spi1 in fission yeast and RCC1/Ran proteins in mammalian cells.
Thomas Merkle +5 more
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Journal of Plant Biotechnology, 2013 Abstract Ran is a small GTP-binding protein that binds and subsequently hydrolyzes GTP. The functions of Ran in nuclear transport and mitotic progression are well conserved in plants and animals. In animal cells, stress treatments cause Ran relocalization and slowing of nuclear transport, but the role of Ran proteins in plant cells exposed to stress is
Young-Hwa Kim, Gyung Hye Huh
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