Ezrin

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Ezrin
Protein VIL2 PDB 1ni2.png
PDB rendering based on 1ni2.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols EZR ; CVIL; CVL; HEL-S-105; VIL2
External IDs OMIM123900 MGI98931 HomoloGene55740 GeneCards: EZR Gene
RNA expression pattern
PBB GE VIL2 208623 s at tn.png
PBB GE VIL2 208621 s at tn.png
PBB GE VIL2 208622 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7430 22350
Ensembl ENSG00000092820 ENSMUSG00000052397
UniProt P15311 P26040
RefSeq (mRNA) NM_001111077 NM_009510
RefSeq (protein) NP_001104547 NP_033536
Location (UCSC) Chr 6:
159.19 – 159.24 Mb
Chr 17:
6.74 – 6.78 Mb
PubMed search [1] [2]

Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.[1]

Structure[edit]

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

Function[edit]

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.[2]

The N-terminal FERM domain strongly binds sodium-hydrogen exchanger regulatory factor (NHERF) proteins (involving long-range allostery).[3] The C-terminal binds to actin, phosphatidylinositol(4,5)bis-phosphate (PIP2)[4]and membrane proteins like CD44 and ICAM-2.

Interactions[edit]

VIL2 has been shown to interact with:

References[edit]

  1. ^ Gould K, Bretscher A, Esch F, 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 401598. PMID 2591371. 
  2. ^ "Entrez Gene: VIL2 villin 2 (ezrin)". 
  3. ^ Farago B, Li J, Cornilescu G, Callaway D, 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 2980739. PMID 21081097. 
  4. ^ Jayasundar J, Ju J, He L, Liu D, Meilleur F, Zhao J et al. (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 3481312. PMID 22927432. 
  5. ^ Serrador J, Nieto M, Alonso-Lebrero J, del Pozo M, Calvo J, Furthmayr H et al. (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. 
  6. ^ 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. 
  7. ^ Parlato S, Giammarioli A, Logozzi M, Lozupone F, Matarrese P, Luciani F et al. (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 302100. PMID 11013215. 
  8. ^ 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. 
  9. ^ Serrador J, Vicente-Manzanares M, Calvo J, Barreiro O, Montoya M, Schwartz-Albiez R et al. (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. 
  10. ^ 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. 
  11. ^ 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 301263. PMID 7579708. 
  12. ^ 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 47875. PMID 8248180. 
  13. ^ 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 22080. PMID 10377409. 
  14. ^ Mykkänen O, Grönholm M, Rönty M, Lalowski M, Salmikangas P, Suila H et al. (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 60155. PMID 11598191. 
  15. ^ 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 194886. PMID 12808036. 
  16. ^ Granés F, Urena J, Rocamora N, Vilaró S (April 2000). "Ezrin links syndecan-2 to the cytoskeleton". J. Cell. Sci. 113 (7): 1267–76. PMID 10704377. 
  17. ^ Brdicková N, Brdicka T, Andera L, Spicka J, Angelisová P, Milgram S et al. (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. 
  18. ^ 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 2139813. PMID 9314537. 
  19. ^ Yun C, Lamprecht G, Forster D, 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. 
  20. ^ Sitaraman S, Wang L, Wong M, Bruewer M, Hobert M, Yun C et al. (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. 
  21. ^ Barreiro O, Yanez-Mo M, Serrador J, Montoya M, Vicente-Manzanares M, Tejedor R et al. (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 2173557. PMID 12082081. 

Further reading[edit]