Upstream and Downstream of Ran GTPase
Abstract
Among the Ras family, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras family. Ran may therefore interact with a wide range of proteins in various intracellular locations. This means that Ran could play many different roles like nucleocytoplasmic transport, microtubule assembly and so on. All of the Ran functions should be regulated by RanGEF and RanGAP. It is an interesting issue why RCC1, a RanGEF, is localized in the nucleus and RanGAP1/Ran1p in the cytoplasm. It is possible that RCC1 checks the state of chromosomal DNA replication and transfers it to the downstream events through Ran; thereby, RCC1 would be involved in coupling the spatial localization of cellular macromolecules with the cell cycle progression. In this context, Ran will be a very important cell cycle mediator. There is yet another G protein cascade, Gtr1-Gtr2, which interacts with the Ran cycle.
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Highlight: GTP Binding Proteins Central Regulators in Cell Biology
- Signal Transduction and Post-Transcriptional Gene Expression
- Regulation of GTPases in the Bacterial Translation Machinery
- GTPase Mechanisms and Functions of Translation Factors on the Ribosome
- The Role of Heterotrimeric G Proteins in Platelet Activation
- Upstream and Downstream of Ran GTPase
- Nogo-A, a Potent Inhibitor of Neurite Outgrowth and Regeneration
- Rho GTPases as Targets of Bacterial Protein Toxins
- A Conserved Gβ Binding (GBB) Sequence Motif in Ste20p/PAK Family Protein Kinases
- Identification of a CpG Island in the Human LRP-2 Gene and Analysis of Its Methylation Status in Parathyroid Adenomas
- Theoretical Description of the Direct Exponential Amplification and Sequencing (DEXAS) Method
- Adenine Nucleotide N-Glycosidase Activity of the A-Chain of Cinnamomin Characterized by 1H-Nuclear Magnetic Resonance
- Msb4p, a Protein Involved in Cdc42p-Dependent Organization of the Actin Cytoskeleton, Is a Ypt/Rab-Specific GAP
- Muscle Phosphorylase Kinase Is Not a Substrate of AMP-Activated Protein Kinase
- Cationic Lipopolyamines Induce Degradation of PrPSc in Scrapie-Infected Mouse Neuroblastoma Cells
- Glycosylphosphatidylinositol-Specific Phospholipase D of Human Serum Activity Modulation by Naturally Occurring Amphiphiles
- Retrieval of the mrp2 Gene Encoded Conjugate Export Pump from the Canalicular Membrane Contributes to Cholestasis Induced by tert-Butyl Hydroperoxide and Chloro-Dinitrobenzene
- Matrix Metalloproteinases-2, -3, -7, -9 and -10, But Not MMP-11, Are Differentially Expressed in Normal, Benign Tumorigenic and Malignant Human Keratinocyte Cell Lines
- Human Keratinocyte Cell Lines Differ in the Expression of the Collagenolytic Matrix Metallo-proteinases-1, -8, and -13 and of TIMP-1
- Inducibility of the Streptomyces traRts107-Ptra Expression Cassette in Mycobacterium smegmatis
- Shortest Known Prion Protein Allele in Highly BSE-Susceptible Lemurs
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