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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.
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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.
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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 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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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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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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Small GTPases.

David J Reiner1, Erik A Lundquist2

  • 1Institute of Biosciences and Technology, Texas A&M Health Science Center, Houston, TX USA.

Wormbook : the Online Review of C. Elegans Biology
|May 25, 2016
PubMed
Summary
This summary is machine-generated.

Small guanosine triphosphatases (GTPases) are crucial molecular switches in cell biology. This study compares small GTPase complements in C. elegans and mammals, revealing conserved and unique members.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genomics

Background:

  • Small guanosine triphosphatases (GTPases) are essential regulators in cellular processes.
  • They function as molecular switches, controlling cell signaling through GTP/GDP binding.
  • The Ras superfamily, including Ras, Rho, Rab, Arf, and Ran families, is conserved across eukaryotes.

Purpose of the Study:

  • To provide an overview of small GTPase biology.
  • To compare the small GTPase repertoire in Caenorhabditis elegans with mammalian counterparts.
  • To identify and discuss atypical nematode small GTPases.

Main Methods:

  • Comparative genomics analysis of small GTPase families.
  • Bioinformatic survey of the C. elegans genome for small GTPase identification.
  • Literature review of small GTPase functions and evolution.

Main Results:

  • C. elegans possesses a complement of small GTPases comparable to other eukaryotes.
  • Functional diversification of small GTPase families has occurred throughout evolution.
  • Atypical nematode-specific small GTPases were identified, expanding the known repertoire.

Conclusions:

  • Small GTPases are fundamental to eukaryotic cell biology with conserved roles.
  • Comparative analysis highlights evolutionary adaptations in small GTPase families.
  • The study expands the understanding of small GTPase diversity and function in nematodes.