Vimentin 1300486 224735664 2008-07-10T05:04:22Z AkhtaBot 6756213 robot Modifying: [[ar:فيمنتين]] {{PBB|geneid=7431}} '''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. == Structure == A vimentin monomer, like all other intermediate filaments, has a central α-helical [[Protein domain|domain]], capped on each end by non-[[helical]] amino (head) and carboxy (tail) end domains.<ref name="fuchs">{{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/annurev.bi.63.070194.002021}}</ref> 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<sup>('''no figure on this page!''')</sup> 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.<ref name="fuchs" /> 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.<ref name="fuchs" /> The spacing of the charged residues is optimal for ionic [[Salt bridge (protein)|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.<ref name="fuchs" /> == Function == Scientists have found that vimentin is attached to the [[cell nucleus|nucleus]], [[endoplasmic reticulum]], and [[mitochondria]], either laterally or terminally.<ref name="katsumoto">{{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}}</ref> They concluded that vimentin plays a significant role in supporting and anchoring the position of the organelles in the [[cytosol]]. [http://cpmcnet.columbia.edu/dept/gsas/anatomy/Faculty/Gundersen/movies.html Vimentin Clips] offers three different clips that beautifully 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.) <ref name="goldman">{{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}}</ref> Results of a study involving [[transgenic]] mice that lacked vimentin<ref name="goldman" /> 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.<ref name="goldman" /> [http://www.kizefo.de/pics/gallery_pict/cytoskeleton/cyt_web_dirk/Dirk_Cytoskeleton.html 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.<ref name="sarria">{{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}}</ref> 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. <ref name="sarria" /> == References == {{reflist}} ==Further reading== {{refbegin | 2}} {{PBB_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= }} *{{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 }} }} {{refend}} {{Cytoskeletal Proteins}} [[Category:Cytoskeleton]] [[Category:Proteins]] <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. --> {{PBB_Controls | update_page = yes | require_manual_inspection = no | update_protein_box = yes | update_summary = no | update_citations = yes }} [[ar:فيمنتين]] [[de:Vimentin]] [[es:Vimentina]] [[fr:Vimentine]] [[ja:ビメンチン]] [[pl:Wimentyna]] [[ru:Виментин]] [[zh:波形蛋白]]