GTPase
class of enzymes
GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved P-loop "G domain", a protein domain common to many GTPases.
Functions
GTPases function as molecular switches or timers in many fundamental cellular processes.
Examples of these roles include:
Signal transduction in response to activation of cell surface receptors, including transmembrane receptors such as those mediating taste, smell and vision.
Protein biosynthesis (a.k.a. translation) at the ribosome.
Regulation of cell differentiation, proliferation, division and movement.
Translocation of proteins through membranes.
Transport of vesicles within the cell, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly.
GTPases are active when bound to GTP and inactive when bound to GDP. In the generalized receptor-transducer-effector signaling model of Martin Rodbell, signaling GTPases act as transducers to regulate the activity of effector proteins.
The public source identifies “GTPase” as class of enzymes. This brief keeps that definition visible, then builds a research path around GTPase, class and enzymes.
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This entry incorporates text from “GTPase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.