Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4

The human Ras-related nuclear protein Ran/TC4 (refs 1-4) is the prototype of a well conserved family of GTPases that can regulate both cell-cycle progression and messenger RNA transport. Ran has been proposed to undergo tightly controlled cycles of GTP binding and hydrolysis, to operate as a GTPase...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1993-12, Vol.366 (6455), p.585-587
Main Authors: Coutavas, Elias, Ren, Mindong, Oppenheim, Joel D, D'Eustachio, Peter, Rush, Mark G
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Biochemistry
Biological and medical sciences
Cell Cycle - physiology
Cell cycle, cell proliferation
Cell physiology
Cloning
Codon
Conserved Sequence
Fundamental and applied biological sciences. Psychology
Genes, ras
Genetics
GTP-Binding Proteins - metabolism
GTPase-Activating Proteins
Guanosine Triphosphate - metabolism
HeLa Cells
Humans
Molecular and cellular biology
Molecular Sequence Data
Mutagenesis, Site-Directed
Nuclear Proteins - biosynthesis
Nuclear Proteins - metabolism
Proteins
Proteins - metabolism
ran GTP-Binding Protein
ras GTPase-Activating Proteins
S100 Proteins - metabolism
Schizosaccharomyces - metabolism
Xenopus
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The human Ras-related nuclear protein Ran/TC4 (refs 1-4) is the prototype of a well conserved family of GTPases that can regulate both cell-cycle progression and messenger RNA transport. Ran has been proposed to undergo tightly controlled cycles of GTP binding and hydrolysis, to operate as a GTPase switch whose GTP- and GDP-bound forms interact differentially with regulators and effectors. One known regulator, the protein RCC1 (refs 12, 13), interacts with Ran to catalyse guanine nucleotide exchange, and both RCC1 and Ran are components of an intrinsic checkpoint control that prevents the premature initiation of mitosis. To test and extend the GTPase-switch model, we searched for a Ran-specific GTPase-activating protein (GAP), and for putative effectors (proteins that interact specifically with Ran/TC4-GTP). We report here the identification of a Ran GAP and its use to characterize the GTP-hydrolysing properties of mutant Ran proteins, and the identification and cloning of a binding protein specific for Ran/TC4-GTP.
ISSN:0028-0836
1476-4687
DOI:10.1038/366585a0