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RESULTS [51 .. 101]
From Wikipedia, the free encyclopedia
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Vimentin

PDB rendering based on 1gk4.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols VIM ; FLJ36605
External IDs OMIM193060 MGI98932 HomoloGene2538 GeneCards: VIM Gene
RNA expression pattern
PBB GE VIM 201426 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7431 22352
Ensembl ENSG00000026025 ENSMUSG00000026728
UniProt P08670 P20152
RefSeq (mRNA) NM_003380 NM_011701
RefSeq (protein) NP_003371 NP_035831
Location (UCSC) Chr 10:
17.27 – 17.28 Mb
Chr 2:
13.57 – 13.58 Mb
PubMed search [1] [2]
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 protein that in humans is encoded by the VIM gene.

Vimentin is a type III intermediate filament (IF) protein that is expressed in mesenchymal cells. IF proteins are found in all metazoan cells[1] as well as bacteria.[2] IF, along with tubulin-based microtubules and actin-based microfilaments, 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-to-mesenchymal transition (EMT) during both normal development and metastatic progression.

Structure[edit]

A vimentin monomer, like all other intermediate filaments, has a central α-helical domain, capped on each end by non-helical amino (head) and carboxyl (tail) domains.[3] Two monomers are likely co-translationally expressed in a way that facilitates their formation of a coiled-coil dimer, which is the basic subunit of vimentin assembly.[4]

The α-helical sequences contain a pattern of hydrophobic amino acids that contribute to forming a "hydrophobic seal" on the surface of the helix.[3] 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.[3] 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.[3]

Function[edit]

Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.[5]

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).[6] Transgenic mice that lacked vimentin[6] are functionally normal. It is possible that the microtubule network may have compensated for the absence of the intermediate network. This result supports an intimate interactions between microtubules and vimentin. Moreover, when microtubule depolymerizers were present, vimentin reorganization occurred, once again implying a relationship between the two systems.[6]

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.[7] 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.[7]

Clinical significance[edit]

It has been used as a sarcoma tumor marker to identify mesenchyme.[8][9]

Vimentin methylation has been established as a biomarker of colon cancer—this marker is being utilized in the development of fecal tests for colon cancer. Statistically significant levels of vimentin methylation have also been observed in certain upper gastrointestinal pathologies such as Barrett's esophagus, esophageal adenocarcinoma, and intestinal type gastric cancer.[10] High levels of DNA methylation in the promotor region have also been associated with markedly decreased survival in hormone positive breast cancers.[11]

See also Anti-citrullinated protein antibody for its use in diagnosis of rheumatoid arthritis.

Interactions[edit]

Vimentin has been shown to interact with:

The 3' UTR of Vimentin mRNA has been found to bind a 46kDa protein.[21]

References[edit]

  1. ^ Eriksson JE, Dechat T, Grin B, Helfand B, Mendez M, Pallari HM, Goldman RD (2009). "Introducing intermediate filaments: from discovery to disease". J Clin Invest 119 (7): 1763–71. doi:10.1172/JCI38339. PMC 2701876. PMID 19587451. 
  2. ^ Cabeen MT, Jacobs-Wagner C (2010). "The bacterial cytoskeleton". Annu Rev Genet 44: 365–92. doi:10.1146/annurev-genet-102108-134845. PMID 21047262. 
  3. ^ a b c d Fuchs E., Weber K. (1994). "Intermediate filaments: structure, dynamics, function, and disease". Annu Rev Biochem 63: pp. 345–82. doi:10.1146/annurev.bi.63.070194.002021. PMID 7979242. 
  4. ^ Chang L, Shav-Tal Y, Trcek T, Singer RH, Goldman RD. (2006). "Assembling an intermediate filament network by dynamic cotranslation". J Cell Biol 172 (5): 747–58. doi:10.1083/jcb.200511033. PMC 2063706. PMID 16505169. 
  5. ^ Katsumoto T., Mitsushima A., Kurimura T. (1990). "The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction". Biol Cell 68 (2): pp. 139–46. doi:10.1016/0248-4900(90)90299-I. PMID 2192768. 
  6. ^ a b c Goldman RD, Khuon S, Chou YH, Opal P, Steinert PM (August 1996). "The function of intermediate filaments in cell shape and cytoskeletal integrity". J. Cell Biol. 134 (4): 971–83. doi:10.1083/jcb.134.4.971. PMC 2120965. PMID 8769421. 
  7. ^ a b Sarria AJ, Panini SR, Evans RM (September 1992). "A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells". J. Biol. Chem. 267 (27): 19455–63. PMID 1527066. 
  8. ^ Leader M, Collins M, Patel J, Henry K (January 1987). "Vimentin: an evaluation of its role as a tumour marker". Histopathology 11 (1): 63–72. doi:10.1111/j.1365-2559.1987.tb02609.x. PMID 2435649. 
  9. ^ "Immunohistochemistry from the Washington Animal Disease Diagnostic laboratory (WADDL)of the College of Veterinary Medicine, Washington State University". Retrieved 2009-03-14. 
  10. ^ Moinova, Helen (April 2012). "Aberrant Vimentin Methylation is Characteristic of Upper GI Pathologies". Cancer Epidemiology Biomarkers Prev 21 (4): 594–600. 
  11. ^ Ulirsch, Jacob (January 2013). "Vimentin DNA methylation predicts survival in breast cancer". Breast Cancer Research and Treatment 137 (2): 383–96. doi:10.1007/s10549-012-2353-5. PMID 23239149. 
  12. ^ Meng JJ, Bornslaeger EA, Green KJ, Steinert PM, Ip W (1997). "Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments". J. Biol. Chem. 272 (34): 21495–503. doi:10.1074/jbc.272.34.21495. PMID 9261168. 
  13. ^ Lopez-Egido J, Cunningham J, Berg M, Oberg K, Bongcam-Rudloff E, Gobl A (2002). "Menin's interaction with glial fibrillary acidic protein and vimentin suggests a role for the intermediate filament network in regulating menin activity". Exp. Cell Res. 278 (2): 175–83. doi:10.1006/excr.2002.5575. PMID 12169273. 
  14. ^ 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 (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  15. ^ 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 (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070. 
  16. ^ Herrmann H, Wiche G (1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin". J. Biol. Chem. 262 (3): 1320–5. PMID 3027087. 
  17. ^ a b Brown MJ, Hallam JA, Liu Y, Yamada KM, Shaw S (2001). "Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin". J. Immunol. 167 (2): 641–5. PMID 11441066. 
  18. ^ Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y, Amano M, Kaibuchi K, Matsuura Y, Azuma I, Inagaki M (1997). "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. doi:10.1006/bbrc.1997.6669. PMID 9175763. 
  19. ^ Russell RL, Cao D, Zhang D, Handschumacher RE, Pizzorno G (2001). "Uridine phosphorylase association with vimentin. Intracellular distribution and localization". J. Biol. Chem. 276 (16): 13302–7. doi:10.1074/jbc.M008512200. PMID 11278417. 
  20. ^ Tzivion G, Luo ZJ, Avruch J (2000). "Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo". J. Biol. Chem. 275 (38): 29772–8. doi:10.1074/jbc.M001207200. PMID 10887173. 
  21. ^ Zehner ZE, Shepherd RK, Gabryszuk J, Fu TF, Al-Ali M, Holmes WM (August 1997). "RNA-protein interactions within the 3 ' untranslated region of vimentin mRNA". Nucleic Acids Res. 25 (16): 3362–70. doi:10.1093/nar/25.16.3362. PMC 146884. PMID 9241253. 

Further reading[edit]

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

External links[edit]

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