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Related Concept Videos

Rab Proteins01:14

Rab Proteins

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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.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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Rab Cascades01:25

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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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Cell Polarization by Rho Proteins01:21

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Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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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.
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Cytoskeletal Coordination in Cell Migration01:32

Cytoskeletal Coordination in Cell Migration

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A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker...
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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
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Related Experiment Video

Updated: Dec 8, 2025

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
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RNA localization and co-translational interactions control RAB13 GTPase function and cell migration.

Konstadinos Moissoglu1, Michael Stueland1, Alexander N Gasparski1

  • 1Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD, USA.

The EMBO Journal
|September 18, 2020
PubMed
Summary

Localizing RAB13 RNA to cell protrusions is crucial for GTPase activation and efficient cell migration, demonstrating how RNA localization controls protein function in migrating cells.

Keywords:
RABIFRAB13RNA localizationantisense oligoco-translational interaction

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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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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • RNA molecules show specific distribution patterns within mammalian cells, but their functional significance remains largely unexplored.
  • Understanding RNA localization is key to deciphering cellular mechanisms controlling protein function and cellular processes.

Purpose of the Study:

  • To investigate the functional role of RNA localization at cellular protrusions in migrating mesenchymal cells.
  • To elucidate the mechanistic consequences of RAB13 RNA localization on RAB13 GTPase activity and cell migration.

Main Methods:

  • Utilized RAB13 RNA as a model system, focusing on its enrichment at peripheral protrusions versus perinuclear protein concentration.
  • Experimentally prevented RAB13 RNA localization to assess its impact on protein distribution, membrane association, GTPase activation, and cell migration.
  • Investigated co-translational association between RAB13 and its exchange factor, RABIF.

Main Results:

  • Preventing RAB13 RNA localization did not affect overall RAB13 protein distribution or membrane association.
  • Peripheral translation of RAB13 RNA was essential for full RAB13 GTPase activation and efficient cell migration.
  • RAB13 translation promoted co-translational association with RABIF at the cell periphery.

Conclusions:

  • RAB13 RNA localization and subsequent peripheral translation are critical for RAB13-RABIF complex formation and GTPase activation.
  • Local translation of RNA in specific subcellular compartments can impart distinct properties to proteins, controlling their function.
  • This study highlights a novel mechanism for regulating protein function through spatially controlled RNA translation during cell migration.