View source for Vimentin

{{short description|Type III intermediate filament protein}}
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{{Infobox_gene}}
[[File:VIMENTIN.jpg|thumb|328px|Immunofluorescence staining pattern of vimentin antibodies. Produced by incubating vimentin primary antibodies and FITC labelled secondary antibodies with HEp-20-10 cells.]]

'''Vimentin''' is a [[structural protein]] that in humans is encoded by the ''VIM'' [[gene]]. Its name comes from the [[Latin]] ''vimentum'' which refers to an array of flexible rods.<ref name="pmid368806">{{cite journal | vauthors = Franke WW, Schmid E, Osborn M, Weber K | title = Different intermediate-sized filaments distinguished by immunofluorescence microscopy | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 75 | issue = 10 | pages = 5034–5038 | date = October 1978 | pmid = 368806 | pmc = 336257 | doi = 10.1073/pnas.75.10.5034 | doi-access = free | bibcode = 1978PNAS...75.5034F }}</ref>

[[File:HeLa_cells_showin_Lamp1_in_red,_vimentin_in_green_and_DNA_in_blue.jpg|thumb|328px|Immunofluorescence staining of [[HeLa | HeLa Cells]] with antibody to reveal vimentin containing intermediate filaments in green and antibody to [[LAMP1]] to reveal lysosomes in red. Nuclear DNA is seen in blue. Antibodies and image courtesy [[EnCor Biotechnology | EnCor Biotechnology Inc]].]]

Vimentin is a [[Intermediate filament#Type III|type III intermediate filament (IF) protein]] that is expressed in [[mesenchymal]] cells. [[Intermediate filament|IF proteins]] are found in all [[Animal|animal cells]]<ref name="Eriksson">{{cite journal | vauthors = Eriksson JE, Dechat T, Grin B, Helfand B, Mendez M, Pallari HM, Goldman RD | title = Introducing intermediate filaments: from discovery to disease | journal = The Journal of Clinical Investigation | volume = 119 | issue = 7 | pages = 1763–1771 | date = July 2009 | pmid = 19587451 | pmc = 2701876 | doi = 10.1172/JCI38339 }}</ref> as well as [[bacteria]].<ref name="Cabeen">{{cite journal | vauthors = Cabeen MT, Jacobs-Wagner C | title = The bacterial cytoskeleton | journal = Annual Review of Genetics | volume = 44 | pages = 365–392 | year = 2010 | pmid = 21047262 | doi = 10.1146/annurev-genet-102108-134845 }}</ref> Intermediate filaments, along with [[tubulin]]-based [[microtubules]] and [[actin]]-based [[microfilament]]s, comprise the [[cytoskeleton]]. All IF proteins are expressed in a highly developmentally-regulated fashion; vimentin is the major cytoskeletal component of [[mesenchymal]] cells. Because of this, vimentin is often used as a marker of mesenchymally-derived cells or cells undergoing an [[Epithelial-mesenchymal transition|epithelial-to-mesenchymal transition]] (EMT) during both normal development and [[Metastasis|metastatic]] progression.

== Structure ==

The assembly of the fibrous vimentin filament that forms the cytoskeleton follows a gradual sequence. The vimentin monomer has a central α-helical [[Protein domain|domain]], capped on each end by non-[[Helix|helical]] amino (head) and carboxyl (tail) domains.<ref name="fuchs">{{cite journal | vauthors = Fuchs E, Weber K | title = Intermediate filaments: structure, dynamics, function, and disease | journal = Annual Review of Biochemistry | volume = 63 | pages = 345–382 | year = 1994 | pmid = 7979242 | doi = 10.1146/annurev.bi.63.070194.002021 }}</ref> Two monomers are likely co-translationally expressed in a way that facilitates their interaction forming a coiled-coil dimer, which is the basic subunit of vimentin assembly.<ref name="chang">{{cite journal | vauthors = Chang L, Shav-Tal Y, Trcek T, Singer RH, Goldman RD | title = Assembling an intermediate filament network by dynamic cotranslation | journal = The Journal of Cell Biology | volume = 172 | issue = 5 | pages = 747–758 | date = February 2006 | pmid = 16505169 | pmc = 2063706 | doi = 10.1083/jcb.200511033 }}</ref> A pair of coiled-coil dimers connect in an [[Antiparallel (biochemistry)|antiparallel]] fashion to form a tetramer. Eight tetramers join to form what is known as the unit-length filament (ULF), ULFs then stick to each other and elongate followed by compaction to form the fibrous proteins.<ref>{{cite journal | vauthors = Danielsson F, Peterson MK, Caldeira Araújo H, Lautenschläger F, Gad AK | title = Vimentin Diversity in Health and Disease | journal = Cells | volume = 7 | issue = 10 | page = 147 | date = September 2018 | pmid = 30248895 | pmc = 6210396 | doi = 10.3390/cells7100147 | doi-access = free }}</ref>

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" /> 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 ==

Vimentin plays a significant role in supporting and anchoring the position of the organelles in the [[cytosol]]. Vimentin is attached to the [[cell nucleus|nucleus]], [[endoplasmic reticulum]], and [[mitochondria]], either laterally or terminally.<ref name="katsumoto">{{cite journal | vauthors = 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 = Biology of the Cell | volume = 68 | issue = 2 | pages = 139–146 | year = 1990 | pmid = 2192768 | doi = 10.1016/0248-4900(90)90299-I | s2cid = 29019928 }}</ref>

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 | vauthors = Goldman RD, Khuon S, Chou YH, Opal P, Steinert PM | title = The function of intermediate filaments in cell shape and cytoskeletal integrity | journal = The Journal of Cell Biology | volume = 134 | issue = 4 | pages = 971–983 | date = August 1996 | pmid = 8769421 | pmc = 2120965 | doi = 10.1083/jcb.134.4.971 }}</ref> [[Transgenic]] mice that lack vimentin appeared normal and did not show functional differences.<ref name="Golucci-Guyon">{{cite journal | vauthors = Colucci-Guyon E, Portier MM, Dunia I, Paulin D, Pournin S, Babinet C | title = Mice lacking vimentin develop and reproduce without an obvious phenotype | journal = Cell | volume = 79 | issue = 4 | pages = 679–694 | date = November 1994 | pmid = 7954832 | doi = 10.1016/0092-8674(94)90553-3 | s2cid = 28146121 }}</ref> It is possible that the microtubule network may have compensated for the absence of the intermediate network. This result supports an intimate interaction 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" /> On the other hand, wounded mice that lack the vimentin gene heal slower than their wild type counterparts.<ref name="Eckes2000">{{cite journal | vauthors = Eckes B, Colucci-Guyon E, Smola H, Nodder S, Babinet C, Krieg T, Martin P | title = Impaired wound healing in embryonic and adult mice lacking vimentin | journal = Journal of Cell Science | volume = 113 | issue = 13 | pages = 2455–2462 | date = July 2000 | pmid = 10852824 | doi = 10.1242/jcs.113.13.2455 }}</ref>

In essence, vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin has been shown to eliminate toxic proteins in [[JUNQ and IPOD]] [[inclusion bodies]] in asymmetric division of mammalian [[Cell culture#List of cell lines|cell lines]].<ref name="pmid24843142">{{cite journal | vauthors = Ogrodnik M, Salmonowicz H, Brown R, Turkowska J, Średniawa W, Pattabiraman S, Amen T, Abraham AC, Eichler N, Lyakhovetsky R, Kaganovich D | title = Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 111 | issue = 22 | pages = 8049–8054 | date = June 2014 | pmid = 24843142 | pmc = 4050583 | doi = 10.1073/pnas.1324035111 | doi-access = free | bibcode = 2014PNAS..111.8049O }}</ref>

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 | vauthors = Sarria AJ, Panini SR, Evans RM | title = A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells | journal = The Journal of Biological Chemistry | volume = 267 | issue = 27 | pages = 19455–19463 | date = September 1992 | pmid = 1527066 | doi = 10.1016/S0021-9258(18)41797-8 | doi-access = free }}</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" />

Vimentin plays a role in [[aggresome]] formation, where it forms a cage surrounding a core of aggregated protein.<ref name="pmid9864362">{{cite journal | vauthors = Johnston JA, Ward CL, Kopito RR | title = Aggresomes: a cellular response to misfolded proteins | journal = The Journal of Cell Biology | volume = 143 | issue = 7 | pages = 1883–1898 | date = December 1998 | pmid = 9864362 | pmc = 2175217 | doi = 10.1083/jcb.143.7.1883 }}</ref>

In addition to its conventional intracellular localisation, vimentin can be found extracellularly. Vimentin can be expressed as a cell surface protein and have suggested roles in immune reactions. It can also be released in phosphorylated forms to the extracellular space by activated [[macrophage]]s, [[astrocyte]]s are also known to release vimentin.<ref>{{cite journal | vauthors = Paulin D, Lilienbaum A, Kardjian S, Agbulut O, Li Z | title = Vimentin: Regulation and pathogenesis | journal = Biochimie | volume = 197 | pages = 96–112 | date = June 2022 | pmid = 35151830 | doi = 10.1016/j.biochi.2022.02.003 | s2cid = 246778685 | doi-access = free }}</ref>

== Clinical significance ==

It has been used as a [[sarcoma]] [[tumor marker]] to identify [[mesenchyme]], though its specificity as a bio marker has been disputed.<ref name="pmid2435649">{{cite journal | vauthors = Leader M, Collins M, Patel J, Henry K | title = Vimentin: an evaluation of its role as a tumour marker | journal = Histopathology | volume = 11 | issue = 1 | pages = 63–72 | date = January 1987 | pmid = 2435649 | doi = 10.1111/j.1365-2559.1987.tb02609.x | s2cid = 34804720 }}</ref><ref>{{cite web|url=http://www.vetmed.wsu.edu/depts_Waddl/ICS.aspx|title=Immunohistochemistry from the Washington Animal Disease Diagnostic laboratory (WADDL)of the College of Veterinary Medicine, Washington State University|access-date=2009-03-14|archive-url=https://web.archive.org/web/20081201043331/http://www.vetmed.wsu.edu/depts_waddl/ICS.aspx|archive-date=2008-12-01}}</ref><ref>{{Cite web| vauthors = Gardner J |date=23 September 2010|title=How to Interpret Vimentin Immunostain|url=https://www.youtube.com/watch?v=UDnp14nnNC4 |archive-url=https://ghostarchive.org/varchive/youtube/20211212/UDnp14nnNC4| archive-date=2021-12-12|url-status=live|website=YouTube}}{{cbignore}}</ref> Vimentin is present in spindle cell squameous cell carcinoma.<ref>{{cite journal | vauthors = Dotto JE, Glusac EJ | title = p63 is a useful marker for cutaneous spindle cell squamous cell carcinoma | journal = Journal of Cutaneous Pathology | volume = 33 | issue = 6 | pages = 413–417 | date = June 2006 | pmid = 16776716 | doi = 10.1111/j.0303-6987.2006.00477.x | s2cid = 38273016 }}</ref><ref>{{cite journal | vauthors = Barrette K, Van Kelst S, Wouters J, Marasigan V, Fieuws S, Agostinis P, van den Oord J, Garmyn M | title = Epithelial-mesenchymal transition during invasion of cutaneous squamous cell carcinoma is paralleled by AKT activation | journal = The British Journal of Dermatology | volume = 171 | issue = 5 | pages = 1014–1021 | date = November 2014 | pmid = 24628329 | doi = 10.1111/bjd.12967 | s2cid = 42440330 }}</ref>

Methylation of the vimentin gene has been established as a biomarker of colon cancer and this is being utilized in the development of fecal tests for colon cancer. Statistically significant levels of vimentin gene methylation have also been observed in certain upper gastrointestinal pathologies such as [[Barrett's esophagus]], esophageal adenocarcinoma, and intestinal type gastric cancer.<ref name="pmid22315367">{{cite journal | vauthors = Moinova H, Leidner RS, Ravi L, Lutterbaugh J, Barnholtz-Sloan JS, Chen Y, Chak A, Markowitz SD, Willis JE | title = Aberrant vimentin methylation is characteristic of upper gastrointestinal pathologies | journal = Cancer Epidemiology, Biomarkers & Prevention | volume = 21 | issue = 4 | pages = 594–600 | date = April 2012 | pmid = 22315367 | pmc = 3454489 | doi = 10.1158/1055-9965.EPI-11-1060 }}</ref> High levels of DNA methylation in the promoter region have also been associated with markedly decreased survival in hormone positive breast cancers.<ref>{{cite journal | vauthors = Ulirsch J, Fan C, Knafl G, Wu MJ, Coleman B, Perou CM, Swift-Scanlan T | title = Vimentin DNA methylation predicts survival in breast cancer | journal = Breast Cancer Research and Treatment | volume = 137 | issue = 2 | pages = 383–396 | date = January 2013 | pmid = 23239149 | pmc = 3838916 | doi = 10.1007/s10549-012-2353-5 }}</ref>
Downregulation of vimentin was identified in cystic variant of [[papillary thyroid carcinoma]] using a proteomic approach.<ref name="pmid25978681">{{cite journal | vauthors = Dinets A, Pernemalm M, Kjellin H, Sviatoha V, Sofiadis A, Juhlin CC, Zedenius J, Larsson C, Lehtiö J, Höög A | title = Differential protein expression profiles of cyst fluid from papillary thyroid carcinoma and benign thyroid lesions | journal = PLOS ONE | volume = 10 | issue = 5 | article-number = e0126472 | date = 2015 | pmid = 25978681 | pmc = 4433121 | doi = 10.1371/journal.pone.0126472 | doi-access = free | bibcode = 2015PLoSO..1026472D }}</ref>
See also [[Anti-citrullinated protein antibody]] for its use in diagnosis of [[rheumatoid arthritis]]. Vimentin has also been found to be an attachment factor for [[SARS-CoV-2]].<ref>{{cite journal | vauthors = Amraei R, Xia C, Olejnik J, White MR, Napoleon MA, Lotfollahzadeh S, Hauser BM, Schmidt AG, Chitalia V, Mühlberger E, Costello CE, Rahimi N | title = Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 119 | issue = 6 | date = February 2022 | pmid = 35078919 | pmc = 8833221 | doi = 10.1073/pnas.2113874119 | doi-access = free | bibcode = 2022PNAS..11913874A | id = e2113874119 }}</ref>

== Interactions ==

Vimentin has been shown to [[Protein-protein interaction|interact]] with: 
* [[Desmoplakin|DSP]]<ref name = pmid9261168>{{cite journal | vauthors = Meng JJ, Bornslaeger EA, Green KJ, Steinert PM, Ip W | title = Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments | journal = The Journal of Biological Chemistry | volume = 272 | issue = 34 | pages = 21495–21503 | date = August 1997 | pmid = 9261168 | doi = 10.1074/jbc.272.34.21495 | doi-access = free }}</ref> 
* [[MEN1]]<ref name = pmid12169273>{{cite journal | vauthors = Lopez-Egido J, Cunningham J, Berg M, Oberg K, Bongcam-Rudloff E, Gobl A | title = Menin's interaction with glial fibrillary acidic protein and vimentin suggests a role for the intermediate filament network in regulating menin activity | journal = Experimental Cell Research | volume = 278 | issue = 2 | pages = 175–183 | date = August 2002 | pmid = 12169273 | doi = 10.1006/excr.2002.5575 }}</ref> 
* [[MYST2]]<ref name = pmid16189514>{{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–1178 | date = October 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | s2cid = 4427026 | author-link30 = Huda Zoghbi | bibcode = 2005Natur.437.1173R }}</ref><ref name = pmid16169070>{{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–968 | date = September 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 | hdl-access = free | s2cid = 8235923 | hdl = 11858/00-001M-0000-0010-8592-0 }}</ref> 
* [[Protein kinase N1|PKN1]]<ref name = pmid9175763>{{cite journal | vauthors = Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y, Amano M, Kaibuchi K, Matsuura Y, Azuma I, Inagaki M | title = Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN | journal = Biochemical and Biophysical Research Communications | volume = 234 | issue = 3 | pages = 621–625 | date = May 1997 | pmid = 9175763 | doi = 10.1006/bbrc.1997.6669 | bibcode = 1997BBRC..234..621M }}</ref> 
* [[PRKCI]]<ref name="pmid29048609">{{cite journal | vauthors = Ratnayake WS, Apostolatos AH, Ostrov DA, Acevedo-Duncan M | title = Two novel atypical PKC inhibitors; ACPD and DNDA effectively mitigate cell proliferation and epithelial to mesenchymal transition of metastatic melanoma while inducing apoptosis | journal = International Journal of Oncology | volume = 51 | issue = 5 | pages = 1370–1382 | date = November 2017 | pmid = 29048609 | pmc = 5642393 | doi = 10.3892/ijo.2017.4131 }}</ref><ref name="pmid29781749">{{cite journal | vauthors = Ratnayake WS, Apostolatos CA, Apostolatos AH, Schutte RJ, Huynh MA, Ostrov DA, Acevedo-Duncan M | title = Oncogenic PKC-ι activates Vimentin during epithelial-mesenchymal transition in melanoma; a study based on PKC-ι and PKC-ζ specific inhibitors | journal = Cell Adhesion & Migration | volume = 12 | issue = 5 | pages = 447–463 | date = 2018 | pmid = 29781749 | pmc = 6363030 | doi = 10.1080/19336918.2018.1471323 }}</ref>
* [[Plectin|PLEC]]<ref name = pmid3027087>{{cite journal | vauthors = Herrmann H, Wiche G | title = Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin | journal = The Journal of Biological Chemistry | volume = 262 | issue = 3 | pages = 1320–1325 | date = January 1987 | pmid = 3027087 | doi = 10.1016/S0021-9258(19)75789-5 | doi-access = free }}</ref><ref name = pmid11441066>{{cite journal | vauthors = Brown MJ, Hallam JA, Liu Y, Yamada KM, Shaw S | title = Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin | journal = Journal of Immunology | volume = 167 | issue = 2 | pages = 641–645 | date = July 2001 | pmid = 11441066 | doi = 10.4049/jimmunol.167.2.641 | doi-access = free }}</ref> 
* [[SPTAN1]]<ref name = pmid11441066/> 
* [[UPP1]]<ref name = pmid11278417>{{cite journal | vauthors = Russell RL, Cao D, Zhang D, Handschumacher RE, Pizzorno G | title = Uridine phosphorylase association with vimentin. Intracellular distribution and localization | journal = The Journal of Biological Chemistry | volume = 276 | issue = 16 | pages = 13302–13307 | date = April 2001 | pmid = 11278417 | doi = 10.1074/jbc.M008512200 | doi-access = free }}</ref>
* [[YWHAZ]]<ref name = pmid10887173>{{cite journal | vauthors = Tzivion G, Luo ZJ, Avruch J | title = Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo | journal = The Journal of Biological Chemistry | volume = 275 | issue = 38 | pages = 29772–29778 | date = September 2000 | pmid = 10887173 | doi = 10.1074/jbc.M001207200 | doi-access = free }}</ref>

The [[Vimentin 3' UTR protein-binding region|3' UTR of Vimentin mRNA]] has been found to bind a 46kDa protein.<ref name="pmid9241253">{{cite journal | vauthors = Zehner ZE, Shepherd RK, Gabryszuk J, Fu TF, Al-Ali M, Holmes WM | title = RNA-protein interactions within the 3 ' untranslated region of vimentin mRNA | journal = Nucleic Acids Research | volume = 25 | issue = 16 | pages = 3362–3370 | date = August 1997 | pmid = 9241253 | pmc = 146884 | doi = 10.1093/nar/25.16.3362 }}</ref>

== References ==
{{Reflist}}

== Further reading ==
{{Refbegin}}
* {{cite journal | vauthors = Snásel J, Pichová I | title = The cleavage of host cell proteins by HIV-1 protease | journal = Folia Biologica | volume = 42 | issue = 5 | pages = 227–230 | year = 1997 | pmid = 8997639 | doi = 10.1007/BF02818986 | s2cid = 7617882 }}
* {{cite journal | vauthors = Lake JA, Carr J, Feng F, Mundy L, Burrell C, Li P | title = The role of Vif during HIV-1 infection: interaction with novel host cellular factors | journal = Journal of Clinical Virology | volume = 26 | issue = 2 | pages = 143–152 | date = February 2003 | pmid = 12600646 | doi = 10.1016/S1386-6532(02)00113-0 }}
{{Refend}}

== External links ==
* [https://web.archive.org/web/20071106044239/http://web.uni-frankfurt.de/fb15/zoologie/kizefo/pics/gallery_pict/cytoskeleton/cyt_web_dirk/Dirk_Cytoskeleton.html Vimentin Images]

{{PDB Gallery|geneid=7431}}
{{Cytoskeletal Proteins}}
{{Tumor markers}}

[[Category:Cytoskeleton]]
[[Category:Cell biology]]
[[Category:Tumor markers]]