Related Experiment Video
Updated: Jul 10, 2026
05:29
Imaging and Quantifying Mitochondrial Morphology in C. elegans During Aging
Published on: January 17, 2025
Vimentin supports mitochondrial morphology and organization
Ho Lam Tang1, Hong Lok Lung, Ka Chun Wu
1Department of Biology, The Chinese University of Hong Kong, Shatin, Hong Kong.
The Biochemical Journal
|November 7, 2007
Summary
Vimentin, an intermediate filament, is crucial for mitochondrial structure and function. Its absence leads to fragmented and disorganized mitochondria, highlighting its role in cellular organization.
Area of Science:
- Cell Biology
- Cytoskeleton Dynamics
- Mitochondrial Biology
Background:
- Vimentin is a key intermediate filament protein providing structural support and influencing organelle positioning within cells.
- Mitochondrial morphology and organization are critical for cellular function and overall health.
- The precise role of vimentin in regulating mitochondrial structure remains incompletely understood.
Purpose of the Study:
- To investigate the contribution of vimentin to mitochondrial morphology and organization.
- To elucidate the interaction between the vimentin cytoskeleton and mitochondria.
Main Methods:
- Subcellular fractionation
- Immunoprecipitation
- Fluorescence microscopy
- Vimentin knockdown experiments
Main Results:
- Vimentin was found to be associated with mitochondria.
- Knockdown of vimentin led to mitochondrial fragmentation, swelling, and disorganization.
- The vimentin cytoskeleton showed significant co-localization and interaction with mitochondria, exceeding that of other cytoskeletal components.
- Evidence suggests vimentin participates in the association of microtubules with mitochondria.
Conclusions:
- Vimentin plays a significant role in maintaining mitochondrial morphology and organization.
- The vimentin cytoskeleton is intimately involved with mitochondria, influencing their structure and potentially their function.
- These findings reveal a novel regulatory relationship between vimentin intermediate filaments and mitochondrial dynamics.
Related Concept Videos
01:39Mitochondrial Protein Sorting
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death. Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
01:45Mitochondrial Membranes
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
01:45Mitochondrial Membranes
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
01:19Translocation 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,...
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,...
01:39Mitochondrial Precursor Proteins
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Most of the mitochondrial precursors...
01:34Protein Transport into the Inner Mitochondrial Membrane
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Transport of mitochondrial precursors across the TIM23 channel is driven by...