Molecular switches
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In the regulation of molecular switches, protein kinases and guanine nucleotide exchange factors(GEF's) turn proteins on and protein phosphotases and GTPase activating proteins(GAP's) turn proteins off.
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Guanine nucleotide-binding proteins regulate a variety of processes, including sensual perception, protein synthesis, various transport processes, and cell growth and differentiation. They act as molecular switches and timers that cycle between inactive guanosine diphosphate (GDP)-bound and active guanosine triphosphate (GTP)-bound states. Recent structural studies show that the switch apparatus itself is a conserved fundamental module but that its regulators and effectors are quite diverse in their structures and modes of interaction. Adenine and guanine nucleoside triphosphates have quite distinct biological roles. Hydrolysis of adenosine triphosphate (ATP) provides energy that drives metabolic reactions by enzymes and movement by motor proteins. Phosphorylation reactions critical to intracellular regulation also consume ATP. With the
possible exception of proteins such as dynamin, septin, tubulin, and elongation factor G, ...
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