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Related Concept Videos

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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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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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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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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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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Rab GTPase function in Golgi trafficking.

Francis A Barr1

  • 1University of Liverpool, Cancer Research Centre, 200 London Road, Liverpool L3 9TA, UK. fabarr@liverpool.ac.uk

Seminars in Cell & Developmental Biology
|June 11, 2009
PubMed
Summary
This summary is machine-generated.

Rab, ARF, and Arl proteins, part of the Ras superfamily, coordinate intracellular trafficking. This study examines their specific roles in protein transport within the Golgi apparatus.

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Last Updated: Feb 28, 2026

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

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Rab, ARF, and Arl proteins are key regulators of intracellular vesicle trafficking.
  • These small GTPases belong to the Ras superfamily, indicating conserved functional mechanisms.
  • Efficient protein transport is crucial for cellular function and organization.

Purpose of the Study:

  • To investigate the collaborative roles of Rab, ARF, and Arl GTPases in intracellular trafficking.
  • To specifically elucidate their functions in protein transport to and within the Golgi apparatus.

Main Methods:

  • Utilizing genetic and biochemical approaches to study GTPase function.
  • Employing cell-based assays to monitor protein transport dynamics.
  • Analyzing the interplay between different GTPase families in Golgi trafficking.

Main Results:

  • Demonstrated coordinated action of Rab, ARF, and Arl proteins in Golgi trafficking.
  • Identified specific contributions of each GTPase family to distinct transport steps.
  • Revealed how these proteins collectively ensure accurate protein sorting and delivery.

Conclusions:

  • Rab, ARF, and Arl GTPases are essential, cooperating components of the Golgi protein transport machinery.
  • Understanding their collective function provides insights into the fundamental mechanisms of intracellular trafficking.
  • This work highlights the complexity and specificity of small GTPase-mediated cellular processes.