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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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, also known...
GTPases and their Regulation02:14

GTPases and their Regulation

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, also known...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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 affinity and are together...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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:
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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 the...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

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Published on: October 8, 2015

How complex is GTPase signaling in trypanosomes?

Mark C Field1, Amanda J O'Reilly

  • 1The Molteno Building, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK. mcf34@cam.ac.uk

Trends in Parasitology
|May 10, 2008
PubMed
Summary

Small GTPase signaling pathways in trypanosomes are less complex than in higher eukaryotes. This study compares GTPase molecules and accessory factors across various genomes to understand trypanosome signaling complexity.

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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Purification of Extracellular Trypanosomes, Including African, from Blood by Anion-Exchangers (Diethylaminoethyl-cellulose Columns)
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Parasitology

Background:

  • Ras-like small GTPases are crucial signaling molecules in higher eukaryotes.
  • Understanding signaling pathways in trypanosomes, parasites causing diseases like sleeping sickness, is vital for therapeutic development.
  • The complexity of small GTPase networks in trypanosomes remains largely unexplored.

Purpose of the Study:

  • To investigate the complexity of small GTPase signaling pathways in trypanosomes.
  • To compare the repertoire of small GTPase molecules and their associated regulatory factors in trypanosomes with other eukaryotes.

Main Methods:

  • Bioinformatic analysis of multiple trypanosome genomes.
  • Comparative genomics to identify and characterize small GTPase families and their accessory proteins.
  • In silico analysis of signaling pathway components.

Main Results:

  • The repertoire of small GTPase molecules in trypanosomes is significantly smaller compared to higher eukaryotes.
  • The diversity and number of accessory factors regulating these GTPases are also reduced in trypanosomes.
  • This suggests a less intricate small GTPase signaling network in trypanosomes.

Conclusions:

  • Trypanosome small GTPase signaling pathways exhibit a simplified architecture relative to those in higher eukaryotes.
  • This comparative genomic approach provides insights into the evolution and functional adaptation of signaling pathways in parasitic organisms.
  • Findings may inform targeted drug discovery efforts against trypanosome-specific signaling vulnerabilities.