Gtp Hydrolysis

Overview

GTP hydrolysis is the chemical reaction in which guanosine triphosphate (GTP) is cleaved into guanosine diphosphate (GDP) and an inorganic phosphate, releasing energy in the process. This reaction is fundamental to cell biology because GTP-binding proteins act as molecular switches: they are active when bound to GTP and switch off when GTP is hydrolysed to GDP. Through this on/off cycle, GTP hydrolysis controls a wide range of cellular processes, including signal transduction, protein synthesis on the ribosome, intracellular vesicle trafficking, and the assembly and disassembly of the cytoskeleton. Enzymes that accelerate this reaction, known as GTPase-activating proteins, provide precise temporal regulation of these pathways. Dynamins, for instance, are large GTPases whose hydrolysis-driven conformational changes help pinch off membrane vesicles during processes such as endocytosis. Research published in this journal addresses membrane and lipid biology relevant to such GTPase machinery, including an analysis of the lipid components in the dynamin fraction prepared from rat brain, which bears on how dynamin-family GTPases interact with cellular membranes. As a discipline, cell biology continues to investigate how GTP hydrolysis times and directs the molecular events that sustain cell function. This page gathers peer-reviewed, open-access research relevant to GTP hydrolysis and cellular regulation.

Research published in this journal

1 peer-reviewed article, ranked by relevance. Each links to its DOI.

This page summarises published research for orientation; it is not medical or professional advice.

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