Biology:Ezrin

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A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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

Structure

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

Function

The cytoplasmic peripheral protein encoded by this gene can be phosphorylated by protein-tyrosine kinase in microvilli and is a member of the ERM protein family. This protein serves as a linker between plasma membrane and actin cytoskeleton. It plays a key role in cell surface structure adhesion, migration, and organization.[2]

The N-terminal domain (also called FERM domain) binds sodium-hydrogen exchanger regulatory factor (NHERF) protein (involving long-range allostery).[3] This binding can happen only when ezrin is in its active state. The activation of ezrin occurs in synergism of the two factors: 1) binding of the N-terminal domain to phosphatidylinositol(4,5)bis-phosphate (PIP2) and 2) phosphorylation of threonine T567 in the C-terminal domain.[4][5] Binding to actin filaments (via C-terminal) and to membrane proteins (via N-terminal) stabilizes the protein's conformation in its active mode. The membrane proteins like CD44 and ICAM-2 are indirect binding partners of ezrin, while EBP50 (ERM binding protein 50) can associate with ezrin directly.[6]

Interactions

VIL2 has been shown to interact with:


References

  1. ↑ "cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1". EMBO J. 8 (13): 4133–42. December 1989. doi:10.1002/j.1460-2075.1989.tb08598.x. PMID 2591371. 
  2. ↑ "Entrez Gene: VIL2 villin 2 (ezrin)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7430. 
  3. ↑ "Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy". Biophysical Journal 99 (10): 3473–82. 2010. doi:10.1016/j.bpj.2010.09.058. PMID 21081097. 
  4. ↑ "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. 2012. doi:10.1074/jbc.M112.380972. PMID 22927432. 
  5. ↑ "Mode of Ezrin-Membrane Interaction as a Function of PIP2 Binding and Pseudophosphorylation". Biophys. J. 110 (12): 2710–2719. 2016. doi:10.1016/j.bpj.2016.05.009. PMID 27332129. 
  6. ↑ "Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes". Immunology 112 (2): 165–176. 2004. doi:10.1111/j.1365-2567.2004.01882.x. PMID 15147559. 
  7. ↑ "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. June 1998. doi:10.1182/blood.V91.12.4632. PMID 9616160. 
  8. ↑ 8.0 8.1 "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. March 2005. doi:10.1074/jbc.M411781200. PMID 15659383. 
  9. ↑ "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. October 2000. doi:10.1093/emboj/19.19.5123. PMID 11013215. 
  10. ↑ 10.0 10.1 10.2 "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. August 1998. doi:10.1074/jbc.273.34.21893. PMID 9705328. 
  11. ↑ "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. March 2002. doi:10.1074/jbc.M110694200. PMID 11784723. 
  12. ↑ "Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin". J. Cell Sci. 112 (6): 895–904. March 1999. PMID 10036239. 
  13. ↑ "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. August 1995. doi:10.1091/mbc.6.8.1061. PMID 7579708. 
  14. ↑ "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. November 1993. doi:10.1073/pnas.90.22.10846. PMID 8248180. 
  15. ↑ "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. June 1999. doi:10.1073/pnas.96.13.7300. PMID 10377409. 
  16. ↑ "Characterization of human palladin, a microfilament-associated protein". Mol. Biol. Cell 12 (10): 3060–73. October 2001. doi:10.1091/mbc.12.10.3060. PMID 11598191. 
  17. ↑ "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P". Mol. Biol. Cell 14 (6): 2372–84. June 2003. doi:10.1091/mbc.E02-09-0553. PMID 12808036. 
  18. ↑ "Ezrin links syndecan-2 to the cytoskeleton". J. Cell Sci. 113 (7): 1267–76. April 2000. PMID 10704377. 
  19. ↑ "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton". FEBS Lett. 507 (2): 133–6. October 2001. doi:10.1016/s0014-5793(01)02955-6. PMID 11684085. 
  20. ↑ "Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family". J. Cell Biol. 139 (1): 169–79. October 1997. doi:10.1083/jcb.139.1.169. PMID 9314537. 
  21. ↑ "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. October 1998. doi:10.1074/jbc.273.40.25856. PMID 9748260. 
  22. ↑ "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. September 2002. doi:10.1074/jbc.M202522200. PMID 12080047. 
  23. ↑ "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. June 2002. doi:10.1083/jcb.200112126. PMID 12082081. 

Further reading





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