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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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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.
Large G-proteins,...
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GTPases and their Regulation02:14

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Small GTPases - Ras and Rho01:24

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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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Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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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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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Rab Cascades01:25

Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Related Experiment Video

Updated: Mar 24, 2026

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

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Review: Translational GTPases.

Cristina Maracci1, Marina V Rodnina1

  • 1Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Goettingen, 37077, Germany.

Biopolymers
|March 15, 2016
PubMed
Summary
This summary is machine-generated.

Translational GTPases (trGTPases) are vital for protein synthesis. Research reveals EF-Tu

Keywords:
EF-TuGTP hydrolysisdecodingribosometRNAtranslation

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Translational GTPases (trGTPases) are essential for protein synthesis on the ribosome.
  • While GTP-binding domains are conserved, GTP hydrolysis and nucleotide exchange rates differ among trGTPases.
  • EF-Tu is a model G protein with rapid, regulated GTPase activity crucial for accurate amino acid incorporation.

Purpose of the Study:

  • To summarize recent advances in understanding the functional cycle and regulation of trGTPases.
  • To highlight insights into EF-Tu's GTPase mechanism and ribosome-catalyzed GTP hydrolysis.
  • To review progress from structural elucidation and reaction mechanism dissection.

Main Methods:

  • Structural elucidation of trGTPases on the ribosome.
  • Dissection of GTPase reaction mechanisms.
  • Analysis of EF-Tu's GTPase activity and its regulation.

Main Results:

  • Recent data provide insights into the GTPase mechanism of EF-Tu.
  • The ribosome acts as an unusual activator, catalyzing GTP hydrolysis.
  • Advances in structural and mechanistic studies have clarified trGTPase function.

Conclusions:

  • Understanding trGTPase function, particularly EF-Tu, is advanced by structural and mechanistic studies.
  • The ribosome's role in catalyzing GTP hydrolysis is a key finding.
  • These insights are crucial for comprehending the forward commitment and energy utilization in translation.