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FLASH GENE
Symbol VIM contributors: mct/npt/pgu - updated : 30-01-2016
HGNC name vimentin
HGNC id 12692
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Cardiovascularheart   highly
Digestiveintestinesmall intestine  highly
Skin/Tegumentskin   highly
Visualeyeanterior segmentcornea  
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Connectivebone   
cell lineage cells of mesenchymal origin
cell lines
fluid/secretion
at STAGE
physiological period embryo, fetal
Text mesenchymal cell, cochlea
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
mono polymer homomer , polymer
HOMOLOGY
interspecies ortholog to murine Vim
homolog to rattus Vim
homolog to Xenopus Xl.127
homolog to zebrafish vim
homolog to C.elegans F55C12.1
Homologene
FAMILY
  • intermediate filament family, type III
  • CATEGORY structural protein
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,mitochondria
    intracellular,cytoplasm,organelle,peroxisome
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    intracellular,cytoplasm,cytosolic
    intracellular,cytoplasm,cytoskeleton,intermed filament
    text
  • vimentin cytoskeleton co-localized and interacted with mitochondria to a greater extent than other cytoskeletal components known to support mitochondria
  • colocalized with VASP and PKG in endothelial cells
  • PPARG colocalized with vimentin in certain organelles, i.e. Golgi, mitochondria and endoplasmic reticulum
  • basic FUNCTION
  • intermediate filament subunit specific for mesenchymal tissue, involved in vascular tuning and wound repair
  • may be an organizer of a number of critical proteins involved in attachment, migration, and cell signaling
  • contribution of vimentin in mitochondrial morphology and organization
  • could participate in the mitochondrial association of microtubules (relatioship between the vimentin-based intermediate filaments and the regulation of mitochondria)
  • important role functional in the maintenance of lens integrity
  • scaffold provided by vimentin is essential for VASP localization and PKG mediated VASP phosphorylation and thus controls endothelial cell migration and proliferation
  • associates with focal adhesion sites which play a dominant role in cell adhesion, cell migration and cell detachment
  • vimentin filaments may play a role in the development of tissue fibrosis by stabilizing collagen mRNAs
  • exhibits a complex pattern of tissue-specific and developmentally regulated expression
  • required for sphingosine 1-phosphate (S1P)- and growth factor (GF)-induced endothelial cell invasion, and vimentin was cleaved by calpains during invasion
  • leucine zipper-containing intermediate filament protein, suppressing ATF4-dependent osteocalcin (Ocn) transcription and osteoblast differentiation
  • plays a pivotal role in epithelial-to-mesenchymal transition and is known to be overexpressed in the prognostically poor basal-like breast cancer subtype
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • vimentin complexed with MMP14 in a manner that required both the cytoplasmic domain of MMP14 and calpain activation, which increased the soluble pool of vimentin in endothelial cells
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacting with GFAP and SYNM in astrocytes
  • interaction between vimentin and VASP constitutes an important step in endothelial cell migration and proliferation
  • binding of AKT1 (tail region) to VIM (head region) results in Vim Ser39 phosphorylation enhancing the ability of VIM to induce motility and invasion while protecting VIMfrom caspase-induced proteolysis
  • LARP6 interacts with vimentin filaments through its La domain and colocalizes with the filaments
  • YY1 is a key transcriptional activator regulating vimentin expression and CpG methylation is sufficient to prevent the binding of YY1 to the vimentin promoter
  • desmin and vimentin, two components of the intermediate filament in muscle, directly interacted with and were degraded by FBXO32 in response to MSTN
  • vimentin binds the ALOX15 promoter and regulates its promoter activity and protein expression
  • NOD2 interacting protein that regulates NOD2 activities including inflammatory NFKB1 signaling, autophagy and bacterial handling
  • TGFB stimulates vimentin production via PI3K-Akt-MTOR signaling, which leads to suppression of ATF4-dependent Ocn transcription and osteoblast differentiation
  • mediates MIR378 function in cellular self-renewal by regulating the expression of the SOX2 transcription factor
  • cytosolic PPARG interacts directly with cytoskeletal vimentin
  • DCN has an impact on the biology of ITGA2B1 integrin and the vimentin intermediate filament system
  • functional linkage between NSMCE3, VIM and FSCN1
  • INVS could upregulate the expression of CDH2, VIM, MMP2, and MMP9
  • TRIM56 is the ubiquitin ligase that is degrading vimentin in Moody cells
  • cell & other
    REGULATION
    Other phosphorylation enhanced during cell division
    ASSOCIATED DISORDERS
    corresponding disease(s) CZP2
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral     --over  
    in breast tumor cells producing unique tubulin-based protrusions when detached from extracellular matrix and with high metastatic potential (significantly increased extension and frequency of microtubule protrusions, the tubulin microtentacles)
    tumoral     --low  
    inhibits migration and invasion of colon and breast cancer cell lines
    tumoral     --over  
    contributes to the aggressive phenotype and poor prognosis in triple-negative breast cancer
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
  • vimentin methylation predicted poor overall survival independent of race, subtype, stage, nodal status, or metastatic disease and holds promise as a new prognostic biomarker for breast cancer patient
  • changes in VIM and FBLN1 methylation levels in cell-free DNA (cfDNA) are associated with Hepatocellular carcinoma (HCC) and could represent useful plasma-based biomarkers
  • positive VIM expression was shown to predict patients' relapse and poor outcome regarding patients' overall survival in laryngeal squamous cell carcinoma
  • Therapy target
    ANIMAL & CELL MODELS