Related Experiment Video
Updated: Jul 29, 2026
08:59
4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Aggresomes, inclusion bodies and protein aggregation.
1Dept of Biological Sciences, Stanford University, Stanford, CA 94305-5020, USA. kopito@stanford.edu
Trends in Cell Biology
|December 21, 2000
Summary
Cells clear toxic protein aggregates using molecular chaperones and proteasomes. Recent findings reveal that animal cells specifically transport these aggregates to inclusion bodies called aggresomes via microtubule-dependent mechanisms.
Area of Science:
- Cell Biology
- Molecular Biology
- Neuroscience
Background:
- Protein aggregate accumulation is implicated in neurodegenerative diseases and systemic amyloidosis.
- Cellular mechanisms like molecular chaperones and proteasomes mitigate toxic protein aggregation.
- Aggregates are often resistant to degradation and form inclusion bodies.
Purpose of the Study:
- To investigate the mechanism of intracellular aggregated protein accumulation.
- To explore the role of cellular transport in the formation of inclusion bodies.
Main Methods:
- Analysis of protein aggregation pathways.
- Microtubule and dynein motor protein function assays.
- Cellular imaging of protein aggregate localization.
Main Results:
- Protein aggregates are not solely accumulated by diffusion.
- Dynein-dependent retrograde transport on microtubules actively delivers aggregates to inclusion bodies.
- This directed transport results in the formation of aggresomes.
Conclusions:
- Aggresome formation is an active, microtubule-dependent process in animal cells.
- Understanding aggresome transport may offer therapeutic targets for proteinopathies.
Related Concept Videos
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:13Cytoskeletal Accessory Proteins
The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
01:38Intralumenal Vesicles and Multivesicular Bodies
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...
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...