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Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
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GTPases and their Regulation02:14

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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
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Activation and Inactivation of G Proteins01:22

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Rab Proteins01:14

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Regulating Rho GTPases and their regulators.

Richard G Hodge1, Anne J Ridley1

  • 1Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.

Nature Reviews. Molecular Cell Biology
|June 16, 2016
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Summary

Rho GTPases are key regulators of cell functions like migration. Beyond simple GTP-GDP cycling, their activity is finely tuned by post-translational modifications and protein interactions, creating a complex regulatory network.

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Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Rho GTPases are critical regulators of cellular processes, including cell migration, polarity, and cell cycle progression.
  • They typically cycle between active (GTP-bound) and inactive (GDP-bound) states to control effector proteins.

Purpose of the Study:

  • To elucidate the complex regulatory mechanisms governing Rho GTPase activity.
  • To highlight the roles of post-translational modifications and protein complexes in Rho GTPase regulation.

Main Methods:

  • Review of existing literature on Rho GTPase signaling pathways.
  • Analysis of regulatory interactions involving guanine nucleotide exchange factors, GTPase-activating proteins, and guanine nucleotide dissociation inhibitors.

Main Results:

  • Rho GTPase regulation extends beyond canonical GTP-GDP cycling.
  • Post-translational modifications and specific protein complex formation significantly influence Rho GTPase activity.
  • Canonical regulators themselves are subject to complex regulatory networks.

Conclusions:

  • Rho GTPase activity is controlled by a sophisticated interplay of factors, including GTP-GDP cycling, post-translational modifications, and protein interactions.
  • Understanding this complex network is crucial for comprehending cellular dynamics and responses.