Related Experiment Video

Updated: Feb 1, 2026

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy
09:29

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy

Published on: May 4, 2016

7.6K

Miro proteins prime mitochondria for Parkin translocation and mitophagy

Dzhamilja Safiulina1, Malle Kuum2, Vinay Choubey2

  • 1Department of Pharmacology, Institute of Biomedicine and Translational Medicine, University of Tartu, Tartu, Estonia dzamilja.safiulina@ut.ee allen.kaasik@ut.ee.

The EMBO Journal
|December 4, 2018
PubMed

Insights

Parkinson

Area of Science:

  • Cell Biology
  • Neuroscience
  • Molecular Biology

Background:

  • Parkinson's disease involves PINK1 and Parkin proteins.
  • Mitochondrial damage triggers ubiquitination and degradation pathways.
  • Miro1 is a GTPase crucial for mitochondrial transport.

Purpose of the Study:

  • To investigate the interaction between Parkin and Miro1 before and after mitochondrial damage.
  • To elucidate the role of Miro1 in Parkin recruitment and mitophagy.
  • To understand the regulatory mechanism of Miro1 ubiquitination by Parkin.

Main Methods:

  • Mitochondrial damage models
  • Protein interaction studies (co-immunoprecipitation)
  • Ubiquitination assays
  • Gene knockdown experiments (siRNA)
  • Confocal microscopy
  • Neuronal cell culture

Main Results:

  • Parkin interacts with Miro1 pre-damage, independent of PINK1 and ubiquitination.
  • Mitochondrial damage and PINK1 activate Parkin, leading to Miro1 ubiquitination and degradation.
  • Miro1 knockdown impairs Parkin translocation and mitophagy.
  • Miro1 EF-hand domains regulate Miro1 ubiquitination and Parkin recruitment.
  • Miro1 protects neurons from glutamate-induced mitophagy.

Conclusions:

  • Miro1 acts as a calcium-sensitive docking site for Parkin on mitochondria.
  • This interaction is critical for mitophagy regulation in response to mitochondrial damage.
  • Miro1's role extends to neuronal protection against excitotoxicity.
Keywords:
Parkincalcium homeostasismiro proteinsmitophagyneuron

More Related Videos

Visualizing Mitophagy with Fluorescent Dyes for Mitochondria and Lysosome07:56

Visualizing Mitophagy with Fluorescent Dyes for Mitochondria and Lysosome

Published on: November 30, 2022

6.1K
Protection of H9c2 Myocardial Cells from Oxidative Stress by Crocetin via PINK1/Parkin Pathway-Mediated Mitophagy07:40

Protection of H9c2 Myocardial Cells from Oxidative Stress by Crocetin via PINK1/Parkin Pathway-Mediated Mitophagy

Published on: May 26, 2023

1.6K

Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.4K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
9.9K
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
636
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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...
6.8K
Peroxisomes and Mitochondria01:30

Peroxisomes and Mitochondria

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.
The peroxisome is a single membrane-bound cellular organelle that can perform several different functions, including lipid metabolism and chemical detoxification. The enzymes within...
95.5K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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...
7.7K