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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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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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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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Mechanism of Lamellipodia Formation01:31

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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Structural basis for Rab6 activation by the Ric1-Rgp1 complex.

J Ryan Feathers1,2, Ryan C Vignogna1, J Christopher Fromme3

  • 1Department of Molecular Biology & Genetics and Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY, 14850, USA.

Nature Communications
|December 5, 2024
PubMed
Summary
This summary is machine-generated.

Researchers elucidated the structure of the Ric1-Rgp1-Rab6 complex, revealing how Rab GTPase activators function. This provides mechanistic insights into Rab6 activation, crucial for organelle homeostasis and membrane trafficking.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • Rab GTPases are key regulators of organelle homeostasis and membrane trafficking.
  • Rab6 specifically controls Golgi cargo flux and is activated by the conserved Ric1-Rgp1 complex.
  • The structural and mechanistic basis of Ric1-Rgp1 function remained uncharacterized.

Purpose of the Study:

  • To determine the structural and mechanistic basis of Rab6 activation by the Ric1-Rgp1 complex.
  • To elucidate the role of specific domains within Ric1-Rgp1 in Rab6 nucleotide exchange.
  • To understand the interaction between Ric1-Rgp1 and Rab6 at a molecular level.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of the Ric1-Rgp1-Rab6 complex.
  • Biochemical assays to identify key residues for Rab6 activation.
  • Structural analysis to characterize protein-protein interactions.

Main Results:

  • The cryo-EM structure of a key intermediate in the nucleotide exchange reaction was determined.
  • Ric1-Rgp1 utilizes an uncharacterized helical RabGEF domain to interact with Rab6's nucleotide-binding domain.
  • An arrestin fold in Ric1-Rgp1 interacts with Rab6's hypervariable domain, suggesting a common binding mechanism for Rab GTPase activators.

Conclusions:

  • The study provides a detailed mechanistic understanding of regulated Rab6 activation at the Golgi.
  • The findings reveal novel structural features of Rab GTPase activators, including a RabGEF domain and an arrestin fold interaction.
  • This work offers insights into conserved mechanisms of organelle homeostasis and membrane trafficking regulation.