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Wikipedia

Ezrin

January 31, 2023

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

EZR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesEZR, CVIL, CVL, HEL-S-105, VIL2, Ezrin
External IDsOMIM: 123900 MGI: 98931 HomoloGene: 55740 GeneCards: EZR
Orthologs
SpeciesHumanMouse
Entrez

7430

22350

Ensembl

ENSG00000092820

ENSMUSG00000052397

UniProt

P15311

P26040

RefSeq (mRNA)

NM_001111077
NM_003379

NM_009510

RefSeq (protein)

NP_001104547
NP_003370

NP_033536

Location (UCSC)Chr 6: 158.77 – 158.82 MbChr 17: 7.01 – 7.05 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[6]

The N-terminal domain (also called FERM domain) binds sodium-hydrogen exchanger regulatory factor (NHERF) protein (involving long-range allostery).[7] 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.[8][9] 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.[10]

Interactions

VIL2 has been shown to interact with:

References

  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:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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. doi:10.1002/j.1460-2075.1989.tb08598.x. PMC 401598. 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. Bibcode:2010BpJ....99.3473F. doi:10.1016/j.bpj.2010.09.058. PMC 2980739. 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 3481312. PMID 22927432.
  9. ^ Shabardina V, Kramer C, Gerdes B, Braunger J, Cordes A, Schaefer J, Mey I, Grill D, Gerke V, Steinem C (2016). "Mode of Ezrin-Membrane Interaction as a Function of PIP2 Binding and Pseudophosphorylation". Biophys. J. 110 (12): 2710–2719. Bibcode:2016BpJ...110.2710S. doi:10.1016/j.bpj.2016.05.009. PMC 4919509. PMID 27332129.
  10. ^ Ivetic A, Ridley AJ (2004). "Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes". Immunology. 112 (2): 165–176. doi:10.1111/j.1365-2567.2004.01882.x. PMC 1782489. PMID 15147559.
  11. ^ 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. doi:10.1182/blood.V91.12.4632. PMID 9616160.
  12. ^ 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.
  13. ^ 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 302100. PMID 11013215.
  14. ^ 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.
  15. ^ 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.
  16. ^ 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. doi:10.1242/jcs.112.6.895. PMID 10036239.
  17. ^ 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.
  18. ^ 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. Bibcode:1993PNAS...9010846G. doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180.
  19. ^ 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. Bibcode:1999PNAS...96.7300G. doi:10.1073/pnas.96.13.7300. PMC 22080. PMID 10377409.
  20. ^ 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 60155. PMID 11598191.
  21. ^ 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.
  22. ^ Granés F, Urena JM, Rocamora N, Vilaró S (April 2000). "Ezrin links syndecan-2 to the cytoskeleton". J. Cell Sci. 113 (7): 1267–76. doi:10.1242/jcs.113.7.1267. PMID 10704377.
  23. ^ 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. S2CID 12676563.
  24. ^ 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.
  25. ^ 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.
  26. ^ 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.
  27. ^ 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 2173557. PMID 12082081.

Further reading

  • Martin TA, Harrison G, Mansel RE, Jiang WG (2004). "The role of the CD44/ezrin complex in cancer metastasis". Crit. Rev. Oncol. Hematol. 46 (2): 165–86. doi:10.1016/S1040-8428(02)00172-5. PMID 12711360.


 

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

January 31, 2023
ezrin, also, known, cytovillin, villin, protein, that, humans, encoded, gene, ezravailable, structurespdbortholog, search, pdbe, rcsblist, codes4rm8, 4rma, 4rm9, 1ni2identifiersaliasesezr, cvil, vil2, external, idsomim, 123900, 98931, homologene, 55740, geneca. Ezrin also known as cytovillin or villin 2 is a protein that in humans is encoded by the EZR gene 5 EZRAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes4RM8 4RMA 4RM9 1NI2IdentifiersAliasesEZR CVIL CVL HEL S 105 VIL2 EzrinExternal IDsOMIM 123900 MGI 98931 HomoloGene 55740 GeneCards EZRGene location Human Chr Chromosome 6 human 1 Band6q25 3Start158 765 741 bp 1 End158 819 368 bp 1 Gene location Mouse Chr Chromosome 17 mouse 2 Band17 17 A1Start7 005 440 bp 2 End7 050 183 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inbronchial epithelial cellganglionic eminenceright uterine tubejejunal mucosaLeft adrenal glandAchilles tendonright lungupper lobe of lungupper lobe of left lungskin of abdomenTop expressed inEpithelium of stomachmucous cell of stomachleft colonintestinal villusileumseminal vesiculapyloric antrumthymusduodenumfourth ventricleMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein domain specific binding protein containing complex binding cytoskeletal protein binding protein kinase A regulatory subunit binding protein kinase A catalytic subunit binding S100 protein binding actin filament binding protein binding cell adhesion molecule binding microtubule binding ATPase binding actin binding RNA binding cadherin binding protein C terminus binding disordered domain specific binding protein kinase A binding identical protein bindingCellular componentcytoplasm cytosol endosome membrane focal adhesion T tubule ruffle Schwann cell microvillus ruffle membrane actin cytoskeleton perinuclear region of cytoplasm cytoskeleton cell projection cytoplasmic side of apical plasma membrane myelin sheath microvillus microspike apical plasma membrane membrane raft extracellular exosome microvillus membrane ciliary basal body filopodium cortical cytoskeleton plasma membrane apical part of cell astrocyte projection intracellular anatomical structure cell cortex brush border actin filament TCR signalosome cell periphery cell body vesicle plasma membrane raft uropod basolateral plasma membrane immunological synapse cell tip fibrillar center extracellular space extrinsic component of membrane protein containing complexBiological processleukocyte cell cell adhesion regulation of organelle assembly sphingosine 1 phosphate receptor signaling pathway negative regulation of p38MAPK cascade actin filament bundle assembly establishment of epithelial cell apical basal polarity positive regulation of multicellular organism growth astral microtubule organization cellular response to cAMP establishment of endothelial barrier microvillus assembly negative regulation of T cell receptor signaling pathway gland morphogenesis cortical microtubule organization positive regulation of protein localization to early endosome positive regulation of early endosome to late endosome transport intestinal D glucose absorption establishment or maintenance of apical basal cell polarity regulation of NIK NF kappaB signaling epithelial cell differentiation regulation of actin cytoskeleton organization negative regulation of transcription by RNA polymerase II positive regulation of protein secretion membrane to membrane docking regulation of cell shape protein kinase A signaling establishment of centrosome localization phosphatidylinositol mediated signaling regulation of cell size actin cytoskeleton reorganization filopodium assembly receptor internalization terminal web assembly axon guidance positive regulation of gene expression negative regulation of ERK1 and ERK2 cascade protein localization to cell cortex regulation of microvillus length protein localization to plasma membrane positive regulation of protein localization to plasma membraneSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez743022350EnsemblENSG00000092820ENSMUSG00000052397UniProtP15311P26040RefSeq mRNA NM 001111077NM 003379NM 009510RefSeq protein NP 001104547NP 003370NP 033536Location UCSC Chr 6 158 77 158 82 MbChr 17 7 01 7 05 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Structure 2 Function 3 Interactions 4 References 5 Further readingStructure EditThe N terminus of ezrin contains a FERM domain which is further subdivided into three subdomains The C terminus contain an ERM domain Function EditThe 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 6 The N terminal domain also called FERM domain binds sodium hydrogen exchanger regulatory factor NHERF protein involving long range allostery 7 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 8 9 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 10 Interactions EditVIL2 has been shown to interact with CD43 11 FASLG 12 13 ICAM 1 14 ICAM2 14 ICAM3 14 15 Merlin 16 MSN 12 17 18 PIK3R1 19 PALLD 20 S100P 21 SDC2 22 SLC9A3R1 23 24 SLC9A3R2 25 26 and VCAM 1 27 References Edit a b c GRCh38 Ensembl release 89 ENSG00000092820 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000052397 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 doi 10 1002 j 1460 2075 1989 tb08598 x PMC 401598 PMID 2591371 Entrez Gene VIL2 villin 2 ezrin 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 Bibcode 2010BpJ 99 3473F doi 10 1016 j bpj 2010 09 058 PMC 2980739 PMID 21081097 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 3481312 PMID 22927432 Shabardina V Kramer C Gerdes B Braunger J Cordes A Schaefer J Mey I Grill D Gerke V Steinem C 2016 Mode of Ezrin Membrane Interaction as a Function of PIP2 Binding and Pseudophosphorylation Biophys J 110 12 2710 2719 Bibcode 2016BpJ 110 2710S doi 10 1016 j bpj 2016 05 009 PMC 4919509 PMID 27332129 Ivetic A Ridley AJ 2004 Ezrin radixin moesin proteins and Rho GTPase signalling in leucocytes Immunology 112 2 165 176 doi 10 1111 j 1365 2567 2004 01882 x PMC 1782489 PMID 15147559 Serrador JM Nieto M Alonso Lebrero JL del Pozo MA Calvo J Furthmayr H Schwartz Albiez R Lozano F Gonzalez Amaro R Sanchez Mateos P Sanchez 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 doi 10 1182 blood V91 12 4632 PMID 9616160 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 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 302100 PMID 11013215 a b c Heiska L Alfthan K Gronholm M Vilja P Vaheri A Carpen 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 Serrador JM Vicente Manzanares M Calvo J Barreiro O Montoya MC Schwartz Albiez R Furthmayr H Lozano F Sanchez 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 Gronholm M Sainio M Zhao F Heiska L Vaheri A Carpen 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 doi 10 1242 jcs 112 6 895 PMID 10036239 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 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 Bibcode 1993PNAS 9010846G doi 10 1073 pnas 90 22 10846 PMC 47875 PMID 8248180 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 Bibcode 1999PNAS 96 7300G doi 10 1073 pnas 96 13 7300 PMC 22080 PMID 10377409 Mykkanen OM Gronholm M Ronty M Lalowski M Salmikangas P Suila H Carpen 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 60155 PMID 11598191 Koltzscher M Neumann C Konig 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 Granes F Urena JM Rocamora N Vilaro S April 2000 Ezrin links syndecan 2 to the cytoskeleton J Cell Sci 113 7 1267 76 doi 10 1242 jcs 113 7 1267 PMID 10704377 Brdickova N Brdicka T Andera L Spicka J Angelisova P Milgram SL Horejsi 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 S2CID 12676563 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 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 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 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 2173557 PMID 12082081 Further reading EditMartin TA Harrison G Mansel RE Jiang WG 2004 The role of the CD44 ezrin complex in cancer metastasis Crit Rev Oncol Hematol 46 2 165 86 doi 10 1016 S1040 8428 02 00172 5 PMID 12711360 This article on a gene on human chromosome 6 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Ezrin amp oldid 1120202649, wikipedia, wiki, book, books, library,

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