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Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
TLDR
The cloned gene encoding a guanine-nucleotide-exchange factor (GEF) for Rap1 is named Epac, which contains a cAMP-binding site and a domain that is homologous to domains of known GEFs for Ras and Rap1 that is regulated directly by cAMP.
The Guanine Nucleotide-Binding Switch in Three Dimensions
TLDR
Underlying principles of guanosine nucleotide–binding proteins regulate a variety of processes, including sensual perception, protein synthesis, various transport processes, and cell growth and differentiation are defined.
Structural insight into filament formation by mammalian septins.
TLDR
The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions.
The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.
TLDR
The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations.
An Acylation Cycle Regulates Localization and Activity of Palmitoylated Ras Isoforms
We show that the specific subcellular distribution of H- and Nras guanosine triphosphate–binding proteins is generated by a constitutive de/reacylation cycle that operates on palmitoylated proteins,
RanGAP1 induces GTPase activity of nuclear Ras-related Ran.
TLDR
A nuclear homodimeric 65-kDa protein, RanGAP1, is described, which is believed to be the immediate antagonist of RCC1 and induces GTPase activity of Ran, but not Ras, by more than 3 orders of magnitude.
The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogue
TLDR
The X-ray crystal structure of the RBD-RBD complex shows that RBD has the ubiquitin superfold and that the structure of RaplA is very similar to that of Ras.
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