Vimentin is a member of the intermediate filament family of proteins. Intermediate filaments are an important structural feature of eukaryotic cells. They, along with microtubules and actin microfilaments, make up the cytoskeleton. Although most intermediate filaments are stable structures, in fibroblasts, vimentin exists as a dynamic structure.


A vimentin monomer, like all other intermediate filaments, has a central α-helical domain, capped on each end by non-helical amino (head) and carboxy (tail) end domains.cite journal |author=Fuchs E., Weber K. |title=Intermediate filaments: structure, dynamics, function, and disease |journal=Annu Rev Biochem |volume=63 |issue= |pages=pp. 345–82 |year=1994 |pmid=7979242 |doi=10.1146/] Two monomers will twist around each other to form a coiled-coil dimer. Two dimers then form a tetramer, which, in turn, form a sheet by interacting with other tetramers. Figure 1(no figure on this page!) shows the step-by-step process by which the filament is assembled.

The α-helical sequences contain a pattern of hydrophobic amino acids that contribute to forming a "hydrophobic seal" on the surface of the helix. This seal allows the two helices to come together and coil. In addition, there is a periodic distribution of acidic and basic amino acids that seems to play an important role in stabilizing coiled-coil dimers. The spacing of the charged residues is optimal for ionic salt bridges, which allows for the stabilization of the α-helix structure. While this type of stabilization is intuitive for intrachain interactions, rather than interchain interactions, scientists have proposed that perhaps the switch from intrachain salt bridges formed by acidic and basic residues to the interchain ionic associations contributes to the assembly of the filament.


Scientists have found that vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.cite journal |author=Katsumoto T., Mitsushima A., Kurimura T. |title=The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction |journal=Biol Cell |volume=68 |issue=2 |pages=pp. 139–46 |year=1990 |pmid=2192768 |doi=10.1016/0248-4900(90)90299-I] They concluded that vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol.

[ Vimentin Clips] offers three different clips that show vimentin movement inside the cell.

The dynamic nature of vimentin is important when offering flexibility to the cell. Scientists found that vimentin provided cells with a resilience absent from the microtubule or actin filament networks, when under mechanical stress "in vivo". Therefore, in general, it is accepted that vimentin is the cytoskeletal component responsible for maintaining cell integrity. (It was found that cells without vimentin are extremely delicate when disturbed with a micropuncture.) cite journal |author=Goldman R. D., Khuon S., Chou Y., Opal P., Steinert P. |title=The function of intermediate filaments in cell shape and cytoskeletal integrity |journal=J Cell Biol |volume=134 |issue=4 |pages=pp. 971–83 |year=1996 |pmid=8769421 |doi=10.1083/jcb.134.4.971]

Results of a study involving transgenic mice that lacked vimentin showed that the mice were functionally normal. While the outcome is a bit surprising, it is possible that the microtubule network may have compensated for the absence of the intermediate network. This strengthens the suggestion of intimate interactions between microtubules and vimentin. Moreover, when microtubule depolymerizers were present, vimentin reorganization occurred, once again implying a relationship between the two systems.

[ Vimentin Images] <= Broken Link| offers a gallery of images in which vimentin and other cytoskeletal structures are labeled. These images allow the visualization of interactions between vimentin and other cytoskeletal components.

In essence, vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions.

Also, vimentin is found to control the transport of low-density lipoprotein, LDL, -derived cholesterol from a lysosome to the site of esterification.cite journal |author=Sarria A. J., Panini S. R., Evans R. M. |title=A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells |journal=J Biol Chem |volume=267 |issue=27 |pages=pp. 19455–63 |year=1992 |pmid=1527066] With the blocking of transport of LDL-derived cholesterol inside the cell, cells were found to store a much lower percentage of the lipoprotein than normal cells with vimentin. This dependence seems to be the first process of a biochemical function in any cell that depends on a cellular intermediate filament network. This type of dependence has ramifications on the adrenal cells, which rely on cholesteryl esters derived from LDL.


Further reading

citations =
*cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227–30 |year= 1997 |pmid= 8997639 |doi=10.1007/BF02818986
*cite journal | author=Lake JA, Carr J, Feng F, "et al." |title=The role of Vif during HIV-1 infection: interaction with novel host cellular factors |journal=J. Clin. Virol. |volume=26 |issue= 2 |pages= 143–52 |year= 2003 |pmid= 12600646 |doi=10.1016/S1386-6532(02)00113-0

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