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Protein VIL2 PDB 1ni2.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases EZR, CVIL, CVL, HEL-S-105, VIL2, Ezrin
External IDs MGI: 98931 HomoloGene: 55740 GeneCards: EZR
Gene location (Human)
Chromosome 6 (human)
Chr. Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for EZR
Genomic location for EZR
Band 6q25.3 Start 158,765,741 bp[1]
End 158,819,412 bp[1]
RNA expression pattern
PBB GE VIL2 208623 s at fs.png

PBB GE VIL2 208622 s at fs.png

PBB GE VIL2 208621 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 6: 158.77 – 158.82 Mb Chr 17: 6.74 – 6.78 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.[5]


The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contain a ERM domain.


The cytoplasmic peripheral membrane protein encoded by this gene functions as a protein-tyrosine kinase substrate in microvilli. As a member of the ERM protein family, this protein serves as an intermediate between the plasma membrane and the actin cytoskeleton. It plays a key role in cell surface structure adhesion, migration, and organization.[6]

The N-terminal FERM domain strongly binds sodium-hydrogen exchanger regulatory factor (NHERF) proteins (involving long-range allostery).[7] The C-terminal binds to actin, phosphatidylinositol(4,5)bis-phosphate (PIP2)[8] and membrane proteins like CD44 and ICAM-2.


VIL2 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000092820 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052397 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Gould KL, Bretscher A, Esch FS, Hunter T (December 1989). "cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1". EMBO J. 8 (13): 4133–42. PMC 401598Freely accessible. PMID 2591371. 
  6. ^ "Entrez Gene: VIL2 villin 2 (ezrin)". 
  7. ^ Farago B, Li J, Cornilescu G, Callaway DJ, Bu Z (2010). "Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy". Biophysical Journal. 99 (10): 3473–82. doi:10.1016/j.bpj.2010.09.058. PMC 2980739Freely accessible. PMID 21081097. 
  8. ^ Jayasundar JJ, Ju JH, He L, Liu D, Meilleur F, Zhao J, Callaway DJ, Bu Z (2012). "Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering". J. Biol. Chem. 287 (44): 37119–33. doi:10.1074/jbc.M112.380972. PMC 3481312Freely accessible. PMID 22927432. 
  9. ^ Serrador JM, Nieto M, Alonso-Lebrero JL, del Pozo MA, Calvo J, Furthmayr H, Schwartz-Albiez R, Lozano F, González-Amaro R, Sánchez-Mateos P, Sánchez-Madrid F (June 1998). "CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts". Blood. 91 (12): 4632–44. PMID 9616160. 
  10. ^ a b Gajate C, Mollinedo F (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. doi:10.1074/jbc.M411781200. PMID 15659383. 
  11. ^ Parlato S, Giammarioli AM, Logozzi M, Lozupone F, Matarrese P, Luciani F, Falchi M, Malorni W, Fais S (October 2000). "CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway". EMBO J. 19 (19): 5123–34. doi:10.1093/emboj/19.19.5123. PMC 302100Freely accessible. PMID 11013215. 
  12. ^ a b c Heiska L, Alfthan K, Grönholm M, Vilja P, Vaheri A, Carpén O (August 1998). "Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate". J. Biol. Chem. 273 (34): 21893–900. doi:10.1074/jbc.273.34.21893. PMID 9705328. 
  13. ^ Serrador JM, Vicente-Manzanares M, Calvo J, Barreiro O, Montoya MC, Schwartz-Albiez R, Furthmayr H, Lozano F, Sánchez-Madrid F (March 2002). "A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting". J. Biol. Chem. 277 (12): 10400–9. doi:10.1074/jbc.M110694200. PMID 11784723. 
  14. ^ Grönholm M, Sainio M, Zhao F, Heiska L, Vaheri A, Carpén O (March 1999). "Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin". J. Cell Sci. 112 (6): 895–904. PMID 10036239. 
  15. ^ Gary R, Bretscher A (August 1995). "Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site". Mol. Biol. Cell. 6 (8): 1061–75. doi:10.1091/mbc.6.8.1061. PMC 301263Freely accessible. PMID 7579708. 
  16. ^ Gary R, Bretscher A (November 1993). "Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins". Proc. Natl. Acad. Sci. U.S.A. 90 (22): 10846–50. doi:10.1073/pnas.90.22.10846. PMC 47875Freely accessible. PMID 8248180. 
  17. ^ Gautreau A, Poullet P, Louvard D, Arpin M (June 1999). "Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway". Proc. Natl. Acad. Sci. U.S.A. 96 (13): 7300–5. doi:10.1073/pnas.96.13.7300. PMC 22080Freely accessible. PMID 10377409. 
  18. ^ Mykkänen OM, Grönholm M, Rönty M, Lalowski M, Salmikangas P, Suila H, Carpén O (October 2001). "Characterization of human palladin, a microfilament-associated protein". Mol. Biol. Cell. 12 (10): 3060–73. doi:10.1091/mbc.12.10.3060. PMC 60155Freely accessible. PMID 11598191. 
  19. ^ Koltzscher M, Neumann C, König S, Gerke V (June 2003). "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P". Mol. Biol. Cell. 14 (6): 2372–84. doi:10.1091/mbc.E02-09-0553. PMC 194886Freely accessible. PMID 12808036. 
  20. ^ Granés F, Urena JM, Rocamora N, Vilaró S (April 2000). "Ezrin links syndecan-2 to the cytoskeleton". J. Cell Sci. 113 (7): 1267–76. PMID 10704377. 
  21. ^ Brdicková N, Brdicka T, Andera L, Spicka J, Angelisová P, Milgram SL, Horejsí V (October 2001). "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton". FEBS Lett. 507 (2): 133–6. doi:10.1016/s0014-5793(01)02955-6. PMID 11684085. 
  22. ^ Reczek D, Berryman M, Bretscher A (October 1997). "Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family". J. Cell Biol. 139 (1): 169–79. doi:10.1083/jcb.139.1.169. PMC 2139813Freely accessible. PMID 9314537. 
  23. ^ Yun CH, Lamprecht G, Forster DV, Sidor A (October 1998). "NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin". J. Biol. Chem. 273 (40): 25856–63. doi:10.1074/jbc.273.40.25856. PMID 9748260. 
  24. ^ Sitaraman SV, Wang L, Wong M, Bruewer M, Hobert M, Yun CH, Merlin D, Madara JL (September 2002). "The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and Ezrin upon agonist stimulation". J. Biol. Chem. 277 (36): 33188–95. doi:10.1074/jbc.M202522200. PMID 12080047. 
  25. ^ Barreiro O, Yanez-Mo M, Serrador JM, Montoya MC, Vicente-Manzanares M, Tejedor R, Furthmayr H, Sanchez-Madrid F (June 2002). "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes". J. Cell Biol. 157 (7): 1233–45. doi:10.1083/jcb.200112126. PMC 2173557Freely accessible. PMID 12082081. 

Further reading[edit]