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GDP remains bound to the inactive GTPase until a GEF binds and stimulates its release. [3] The localization of GEFs can determine where in the cell a particular GTPase will be active. For example, the Ran GEF, RCC1, is present in the nucleus while the Ran GAP is present in the cytosol, modulating nuclear import and export of proteins. [8]
Rap guanine nucleotide exchange factor (GEF) 4 (RAPGEF4), also known as exchange protein directly activated by cAMP 2 (EPAC2) is a protein that in humans is encoded by the RAPGEF4 gene. [ 5 ] [ 6 ] [ 7 ]
Type IV hypersensitivity, in the Gell and Coombs classification of allergic reactions, often called delayed-type hypersensitivity, is a type of hypersensitivity reaction that can take a day or more to develop. [1] Unlike the other types, it is not humoral (not antibody-mediated) but rather is a type of cell-mediated response.
In plant immunology, the hypersensitive response (HR) is a mechanism used by plants to prevent the spread of infection by microbial pathogens.HR is characterized by the rapid death of cells in the local region surrounding an infection and it serves to restrict the growth and spread of pathogens to other parts of the plant.
Reaction of GeF 4 with fluoride sources produces GeF 5 − anions with octahedral coordination around Ge atom due to polymerization. [6] The structural characterization of a discrete trigonal bipyramidal GeF 5 − anion was achieved by a "naked" fluoride reagent 1,3-bis(2,6-diisopropylphenyl)imidazolium fluoride.
The inactive form of GTPases (GDP-form) are activated by a class of proteins called Guanosine nucleotide exchange factors (GEFs). GEFs catalyse nucleotide exchange by encouraging the release of GDP from the small GTPase (by displacement of the small GTPase-associated Mg 2+ ion) and GDP's replacement by GTP (which is in at least a 10-fold excess within the cell) .
The signal that starts the MAPK/ERK pathway is the binding of extracellular mitogen to a cell surface receptor.This allows a Ras protein (a Small GTPase) to swap a GDP molecule for a GTP molecule, flipping the "on/off switch" of the pathway.
[4] RGS domains in the G protein-coupled receptor kinases are able to bind to Gq family α-subunits, but do not accelerate their GTP hydrolysis. Instead, GRKs appear to reduce Gq signaling by sequestering the active α-subunits away from effectors such as phospholipase C-β.