PI4P-Containing Vesicles from Golgi Contribute to Mitochondrial Division by Coordinating with Polymerized Actin
Related Experiment Video
Updated: Aug 3, 2025

In Vitro Polymerization of F-actin on Early Endosomes
Published on: August 28, 2017
Xinxin Duan1, Yunfei Wei1, Meng Zhang1
1Britton Chance Center for Biomedical Photonics-MoE Key Laboratory for Biomedical Photonics, Advanced Biomedical Imaging Facility-Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China.
Abstract:
Golgi-derived PI4P-containing vesicles play important roles in mitochondrial division, which is essential for maintaining cellular homeostasis. However, the mechanism of the PI4P-containing vesicle effect on mitochondrial division is unclear. Here, we found that actin appeared to polymerize at the contact site between PI4P-containing vesicles and mitochondria, causing mitochondrial division. Increasing the content of PI4P derived from the Golgi apparatus increased actin polymerization and reduced the length of the mitochondria, suggesting that actin polymerization through PI4P-containing vesicles is involved in PI4P vesicle-related mitochondrial division. Collectively, our results support a model in which PI4P-containing vesicles derived from the Golgi apparatus cooperate with actin filaments to participate in mitochondrial division by contributing to actin polymerization, which regulates mitochondrial dynamics. This study enriches the understanding of the pathways that regulate mitochondrial division and provides new insight into mitochondrial dynamics.
Insights
Golgi-derived vesicles containing PI4P (phosphatidylinositol 4-phosphate) drive mitochondrial division by promoting actin polymerization at contact sites. This process is crucial for maintaining cellular homeostasis and mitochondrial dynamics.
Area of Science:
- Cell Biology
- Mitochondrial Dynamics
Background:
- Golgi-derived vesicles containing PI4P are known to be involved in mitochondrial division.
- The precise mechanism by which these vesicles influence mitochondrial division remains largely unknown.
Purpose of the Study:
- To elucidate the mechanism by which PI4P-containing vesicles mediate mitochondrial division.
- To investigate the role of actin polymerization in this process.
Main Methods:
- Observation of vesicle-mitochondria interactions.
- Analysis of actin polymerization at contact sites.
- Manipulation of PI4P levels and assessment of mitochondrial morphology.
Main Results:
- Actin polymerization was observed at the interface between PI4P-containing vesicles and mitochondria, triggering mitochondrial division.
- Elevated levels of Golgi-derived PI4P enhanced actin polymerization.
- Increased actin polymerization correlated with reduced mitochondrial length, indicating fragmentation.
Conclusions:
- PI4P-containing vesicles from the Golgi apparatus collaborate with actin filaments to drive mitochondrial division.
- Actin polymerization, facilitated by these vesicles, is a key regulator of mitochondrial dynamics.
- This study provides novel insights into the regulation of mitochondrial division and cellular homeostasis.
Related Concept Videos
Distribution of Cytoplasmic Content
Distribution of cytoplasmic determinants
The cytoplasm contains various organelles, as well as salts, proteins, and water. The distribution of...
Mechanism of Filopodia Formation
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Coat Assembly and GTPases
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...
The Movement of Organelles and Vesicles
Mechanism of Lamellipodia Formation
Porin Insertion in the Outer Mitochondrial Membrane
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...

