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Intracellular transport based on actin polymerization
1Institute of Cytology, Russian Academy of Sciences, St. Petersburg, 194064, Russia. skhspb@gmail.com.
Biochemistry. Biokhimiia
|November 12, 2014
Summary
The cell uses two actin-based transport systems: actomyosin, driven by myosin, and a unique polymerization system. This polymerization system, crucial for moving particles like vesicles and bacteria, relies on actin polymerization and specific proteins.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Biology
Background:
- Intracellular transport relies on microtubule-based systems and two distinct actin-based systems.
- Actin-based transport involves either myosin motor proteins or unidirectional actin polymerization.
- The actin polymerization system utilizes proteins like WASP/Scar and Arp2/3, forming 'comet-like tails' for cargo movement.
Purpose of the Study:
- To review current understanding of actin polymerization and its regulation.
- To elucidate the mechanisms of intracellular actin-based vesicular transport.
- To highlight the role of actin-binding proteins in cellular transport.
Main Methods:
- Review of existing literature on intracellular transport mechanisms.
- Analysis of high-performance electron microscopy and electron tomography data.
- Examination of cell-free systems, including Xenopus oocyte extracts.
Main Results:
- Two actin-based transport systems exist: actomyosin (myosin-driven) and non-myosin (actin polymerization-driven).
- Actin polymerization forms 'comet-like tails' responsible for moving bacteria, vesicles, and phagosomes.
- This mechanism is essential for various cellular processes, including membrane raft transport and nuclear spindle positioning.
Conclusions:
- Actin polymerization is a key driver of intracellular transport, independent of motor proteins.
- Proteins of the WASP/Scar family and Arp2/3 complex are critical for actin-based transport.
- Understanding these actin-based systems provides insights into fundamental cellular mechanics and disease processes.
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