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]
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
doaj +7 more sources
Two Putative Cypovirus-Encoded miRNAs Co-regulate the Host Gene of GTP-Binding Nuclear Protein Ran and Facilitate Virus Replication [PDF]
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
doaj +5 more sources
Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. [PDF]
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
semanticscholar +5 more sources
Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation [PDF]
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
semanticscholar +4 more sources
Yrb4p, a yeast Ran-GTP-binding protein involved in import of ribosomal protein L25 into the nucleus [PDF]
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+7 more
semanticscholar +7 more sources
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]
Background: Ranbp2 and its Ran-GTP-binding domains' roles in RPE survival/function, a multidisease target, are elusive. Results: RPE undergoes degeneration, disruptions of proteostasis of Ranbp2 partners, and blood-retinal barrier upon Ranbp2 ablation ...
Hemangi Patil+10 more
semanticscholar +6 more sources
Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis. [PDF]
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 ...
Meng Ren+3 more
semanticscholar +6 more sources
Molecular cloning and DNA sequence of a Dictyostelium cDNA encoding a Ran/TC4 related GTP binding protein belonging to the ras superfamily [PDF]
The human gene TC4/ran (also called spi in yeast) codes for a small molecular weight GTPase belonging to the ras superfamily (1, 2, 3, 4). Unlike other members of the ras superfamily which play a variety of roles in the cytoplasm including the regulation
John Bush, James A. Cardelli
semanticscholar +5 more sources
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]
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
semanticscholar +5 more sources