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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Post-translational Translocation of Proteins to the RER01:27

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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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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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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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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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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Related Experiment Video

Updated: Nov 19, 2025

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
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Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

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LRRK2 Modulates the Exocyst Complex Assembly by Interacting with Sec8.

Milena Fais1, Giovanna Sanna1, Manuela Galioto1

  • 1Department of Biomedical Sciences, University of Sassari, 07100 Sassari, Italy.

Cells
|January 27, 2021
PubMed
Summary
This summary is machine-generated.

Mutations in Leucine-Rich Repeat Kinase 2 (LRRK2) are linked to Parkinson's disease. This study reveals LRRK2 interacts with the exocyst complex, impacting vesicle trafficking and potentially Parkinson's disease progression.

Keywords:
LRRK2Parkinson’s diseaseSec8exocyst complex

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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Assaying the Kinase Activity of LRRK2 in vitro
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Related Experiment Videos

Last Updated: Nov 19, 2025

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Assaying the Kinase Activity of LRRK2 in vitro
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Assaying the Kinase Activity of LRRK2 in vitro

Published on: January 18, 2012

22.8K

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Mutations in Leucine-Rich Repeat Kinase 2 (LRRK2) are a significant genetic factor in Parkinson's disease (PD).
  • The precise function of LRRK2 in PD pathogenesis and neuronal function is not fully understood.
  • Emerging evidence suggests LRRK2 influences vesicle trafficking, possibly through Rab phosphorylation.

Purpose of the Study:

  • To investigate the interaction between LRRK2 and the exocyst complex.
  • To elucidate the role of LRRK2 kinase activity in regulating exocyst complex assembly.
  • To explore the functional consequences of this interaction on neuronal physiology and PD.

Main Methods:

  • Co-immunoprecipitation assays to detect LRRK2-Sec8 interaction.
  • In vitro kinase assays to assess LRRK2 activity on exocyst subunits.
  • Cell-based assays to evaluate the impact of LRRK2 and Sec8 expression on cellular phenotypes.

Main Results:

  • Demonstrated a direct interaction between LRRK2 and Sec8, a component of the exocyst complex.
  • Showed that LRRK2 kinase activity regulates the assembly of exocyst subunits.
  • Found that over-expression of Sec8 can rescue pathological effects associated with the LRRK2 G2019S mutation.

Conclusions:

  • LRRK2 kinase activity and its kinase domain are critical for regulating exocyst complex assembly.
  • The interaction between LRRK2 and the exocyst complex provides a novel mechanism for LRRK2 in modulating vesicle trafficking.
  • These findings offer new insights into the molecular underpinnings of LRRK2 in Parkinson's disease.