Guanosine diphosphate , signal

G proteins comprise several families of diverse cellular proteins that subserve an equally diverse array of cellular functions. These proteins derive their name from the fact that they bind the guanine nucleotides guanosine triphosphate (GTP) and guanosine diphosphate (GDP) and possess intrinsic GTPase activity. G proteins play a central role in signal transduction as well as in a myriad of cellular processes, including membrane vesicle transport,... 

All GTP binding proteins in signal transduction share a common structural element - the Ras-like domain which is responsible for the specific complexation of guanosine diphosphate and -triphosphate and which contains catalytic residues that promote GTP-hydrolysis. 

G protein A guanosine triphosphate (GTP)-binding protein that serves as a transducer in a signal transduction pathway. On binding GTP and releasing guanosine diphosphate (GDP), a G protein is able to activate the effector enzyme (e.g., adenylate cyclase). 

Fig. 11. Modes of action of fluorine on osteoblastic cells, (a) Tyrosine phosphatase hypothesis in osteoblastic cells, fluoride ion directly inhibits tyrosine phosphatase. Inhibition of this enzyme enhances the tyrosine phosphorylation of signalling molecules induced by receptor tyrosine kinase, which leads to activation of the extracellular signal-regulated kinase (ERK) through the Ras pathway and enhanced cell proliferation, (b) G-protein hypothesis in osteoblast-like cells, fluoride ions form a complex with aluminum, probably fluoroaluminate, which interacts with guanosine 5 -diphosphate (GDP) to form guanosine 5 -triphosphate (GTP)-like molecule. Activation of the G, protein stimulates the tyrosine phosphorylation of signalling molecules by a yet unknown tyrosine kinase (Tyr Kin) and activation of the ERK kinase through the Ras pathway leads to enhanced cell proliferation. (Reproduced by permission of Elsevier from Ref. [175] ...

The presence of a nitrogen-containing side chain facilitates interaction with the catalytic site of FPPS, an enzyme in the metabolic pathway that is required for the production of the isoprenoid hpids farnesyl diphosphate and geranylgeranyl diphosphate, essential metabolites for posttranslational protein prenylation [5, 8]. Inhibiting the prenylation of guanosine triphosphate-binding proteins such as Ras, Rho, and Rac disrupts the normal cellular signal transduction that is required for osteoclast function and survival [5]. 

Fig. 1. Classical AR signaling. (A) In the absence of agonist, ARs are in the low-affinity state, and G proteins form a heterotrimeric complex bound to guanosine 5 -diphosphate (GDP). Ligand binding allows the formation of a transient complex of activated receptor and G protein. GDP is released from G proteins and is replaced by guanosine 5 -triphosphate (GTP). (B) This leads to dissociation of G proteins into Ga-and G -subunits and activation. Both subunits are able to activate different effectors. (See Color Plate 2 following p. 148.)...

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