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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

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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Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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Gene Regulation During Sporulation01:17

Gene Regulation During Sporulation

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Sporulation is a complex developmental process that allows certain Gram-positive bacteria, such as Bacillus subtilis and Clostridium species, to survive extreme environmental conditions. This process is tightly regulated by a series of signaling cascades and transcriptional controls, ensuring the formation of a highly resistant endospore.Sporulation is triggered by unfavorable conditions, such as nutrient depletion, and is governed by a phosphorelay system. One of the sensor kinases, such as...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Stringent Response in E. coli01:23

Stringent Response in E. coli

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Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
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A Non-Coding Small RNA MicC Contributes to Virulence in Outer Membrane Proteins in Salmonella Enteritidis
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A Non-Coding Small RNA MicC Contributes to Virulence in Outer Membrane Proteins in Salmonella Enteritidis

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Salmonella effector SopD2 interferes with Rab34 function.

Wei Xuan Teo1, Zhe Yang1, Markus Charles Kerr1

  • 1Institute for Molecular Biosciences, University of Queensland, St. Lucia, QLD, 4072, Australia.

Cell Biology International
|February 11, 2017
PubMed
Summary
This summary is machine-generated.

Salmonella SopD2 effector protein binds Rab34, delaying Salmonella Containing Vacuole maturation and inhibiting bacterial growth. This interaction is crucial for Salmonella typhimurium virulence within host cells.

Keywords:
Rab34SalmonellaSopD2host-pathogen interaction

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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Area of Science:

  • Microbiology
  • Cell Biology
  • Immunology

Background:

  • Intracellular pathogens like Salmonella evade host immunity using specialized mechanisms.
  • Salmonella employs type 3 secretion systems (T3SSs) to deliver effectors, subverting host cell processes.
  • The SPI-2 effector SopD2 is known to modulate several Rab GTPases involved in membrane trafficking.

Purpose of the Study:

  • To investigate the interaction between Salmonella effector SopD2 and Rab GTPase family members.
  • To determine the role of Rab34 in the context of Salmonella infection and SopD2 function.
  • To elucidate the impact of SopD2-Rab34 modulation on Salmonella virulence.

Main Methods:

  • Investigated SopD2 binding to Rab34 using biochemical assays.
  • Utilized cell depletion strategies to assess the impact of Rab34 on Salmonella Containing Vacuole (SCV) maturation.
  • Quantified intracellular Salmonella enterica serotype typhimurium (S. typhimurium) growth in manipulated host cells.

Main Results:

  • Demonstrated that SopD2 directly binds and modulates the function of Rab34.
  • Depletion of Rab34 was shown to delay SCV maturation, consequently inhibiting intracellular S. typhimurium growth.
  • S. typhimurium lacking SopD2 exhibited severely impaired growth in Rab34-depleted cells, indicating a synergistic effect on virulence.

Conclusions:

  • Identified Rab34 as a novel Rab GTPase target modulated by the Salmonella effector SopD2.
  • Established Rab34's role in SCV maturation and its contribution to intracellular Salmonella growth.
  • Highlighted a compounding virulence effect when both SopD2 and Rab34 are compromised, offering new insights into Salmonella pathogenesis.