Ezryna

Ezryna (cytowilina, vilin-2; symbole: EZR, CVIL, CVL i VIL2) – białko występujące w ludzkim organizmie kodowane przez gen EZR znajdujący się na chromosomie 6 (locus 6q25.3).

Jest to białko łączące mikrofilamenty budujące mikrokosmki. Ezryna jest obok radyksyny i moezyny częścią rodziny białek ERM które pełnią rolę molekularnych łączników między filamentami aktynowymi a białkami zakotwiczonymi w plazmalemmie. Ezryna odgrywa kluczową rolę w regulowaniu adhezji i polaryzacji komórek.

W okolicy N-końca tego białka zlokalizowana jest domena FERM (four-point one, ezrin/radixin/moesin) która oddziałuje z fosfatydyloinozytol-4,5-bisfosforanu oraz białkami peryferyjnymi takimi jak CD44 i ICAM-2. Na C-końcu znajdują się trzy subdomeny z których jedna oddziałuje z FERM.

Stwierdzone oddziaływania

Zaobserwowano interakcję pomiędzy ezryną a następującymi cząsteczkami: kofaktror 2 NERF, Merlin, SDC2, CD43, Fas ligand, VCAM-1, S100P, ICAM3, ICAM-1, EBP50, ICAM2, Moezyna, PALLD oraz PIK3R1.

Przypisy

↑ William JamesW.J. Smith William JamesW.J., NicolasN. Nassar NicolasN., AnthonyA. Bretscher AnthonyA., Richard A.R.A. Cerione Richard A.R.A., P. AndrewP.A. Karplus P. AndrewP.A., Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions, „Journal of Biological Chemistry”, 278 (7), 2003, s. 4949–4956, DOI: 10.1074/jbc.M210601200, PMID: 12429733 (ang.).
↑ EZR [online], NCBI [dostęp 2020-03-29] (ang.).
↑ AgnieszkaA. Hałoń AgnieszkaA., PiotrP. Donizy PiotrP., Rodzina białek ERM (ezrin/radixin/moesin) – rola i znaczenie w procesach polaryzacji, adhezji i mobilności komórkowej, „Postepy Higieny I Medycyny Doswiadczalnej”, 66, 2012, s. 158–164, DOI: 10.5604/17322693.987628, PMID: 22470191 .
↑ C.H.C.H. Yun C.H.C.H., G.G. Lamprecht G.G., D.V.D.V. Forster D.V.D.V., A.A. Sidor A.A., NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na⁺/H⁺ exchanger NHE3 and the cytoskeletal protein ezrin, „Journal of Biological Chemistry”, 273 (40), 1998, s. 25856–25863, DOI: 10.1074/jbc.273.40.25856, PMID: 9748260 (ang.).
↑ Shanthi V.S.V. Sitaraman Shanthi V.S.V., LixinL. Wang LixinL., MichelleM. Wong MichelleM., MatthiasM. Bruewer MatthiasM., MichaelM. Hobert MichaelM., The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and Ezrin upon agonist stimulation, „Journal of Biological Chemistry”, 277 (36), 2002, s. 33188–33195, DOI: 10.1074/jbc.M202522200, PMID: 12080047 (ang.).
↑ M.M. Grönholm M.M., M.M. Sainio M.M., F.F. Zhao F.F., L.L. Heiska L.L., A.A. Vaheri A.A., Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin, „Journal of Cell Science”, 112 (6), 1999, s. 895–904, PMID: 10036239 (ang.).
↑ F.F. Granés F.F., J.M.J.M. Urena J.M.J.M., N.N. Rocamora N.N., S.S. Vilaró S.S., Ezrin links syndecan-2 to the cytoskeleton, „Journal of Cell Science”, 113 (7), 2000, s. 1267–1276, PMID: 10704377 (ang.).
↑ J.M.J.M. Serrador J.M.J.M., M.M. Nieto M.M., J.L.J.L. Alonso-Lebrero J.L.J.L., M.A. delM.A. Pozo M.A. delM.A., J.J. Calvo J.J., CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts, „Blood”, 91 (12), 1998, s. 4632–4644, DOI: 10.1182/blood.V91.12.4632, PMID: 9616160 (ang.).
1 2 ConsueloC. Gajate ConsueloC., FaustinoF. Mollinedo FaustinoF., Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy, „Journal of Biological Chemistry”, 280 (12), 2005, s. 11641–11647, DOI: 10.1074/jbc.M411781200, PMID: 15659383 (ang.).
↑ S.S. Parlato S.S., A.M.A.M. Giammarioli A.M.A.M., M.M. Logozzi M.M., F.F. Lozupone F.F., P.P. Matarrese P.P., CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway, „The EMBO Journal”, 19 (19), 2000, s. 5123–5134, DOI: 10.1093/emboj/19.19.5123, PMID: 11013215, PMCID: PMC302100 (ang.).
↑ OlgaO. Barreiro OlgaO., MariaM. Yanez-Mo MariaM., Juan M.J.M. Serrador Juan M.J.M., Maria C.M.C. Montoya Maria C.M.C., MiguelM. Vicente-Manzanares MiguelM., Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes, „The Journal of Cell Biology”, 157 (7), 2002, s. 1233–1245, DOI: 10.1083/jcb.200112126, PMID: 12082081, PMCID: PMC2173557 (ang.).
↑ MaxM. Koltzscher MaxM., ClaudiaC. Neumann ClaudiaC., SimoneS. König SimoneS., VolkerV. Gerke VolkerV., Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P, „Molecular Biology of the Cell”, 14 (6), 2003, s. 2372–2384, DOI: 10.1091/mbc.e02-09-0553, PMID: 12808036, PMCID: PMC194886 (ang.).
1 2 3 L.L. Heiska L.L., K.K. Alfthan K.K., M.M. Grönholm M.M., P.P. Vilja P.P., A.A. Vaheri A.A., Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate, „Journal of Biological Chemistry”, 273 (34), 1998, s. 21893–21900, DOI: 10.1074/jbc.273.34.21893, PMID: 9705328 (ang.).
↑ Juan M.J.M. Serrador Juan M.J.M., MiguelM. Vicente-Manzanares MiguelM., JavierJ. Calvo JavierJ., OlgaO. Barreiro OlgaO., Maria C.M.C. Montoya Maria C.M.C., A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting, „Journal of Biological Chemistry”, 277 (12), 2002, s. 10400–10409, DOI: 10.1074/jbc.M110694200, PMID: 11784723 (ang.).
↑ N.N. Brdicková N.N., T.T. Brdicka T.T., L.L. Andera L.L., J.J. Spicka J.J., P.P. Angelisová P.P., Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton, „FEBS Letters”, 507 (2), 2001, s. 133–136, DOI: 10.1016/s0014-5793(01)02955-6, PMID: 11684085 (ang.).
↑ D.D. Reczek D.D., M.M. Berryman M.M., A.A. Bretscher A.A., Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family, „The Journal of Cell Biology”, 139 (1), 1997, s. 169–179, DOI: 10.1083/jcb.139.1.169, PMID: 9314537, PMCID: PMC2139813 (ang.).
↑ R.R. Gary R.R., A.A. Bretscher A.A., Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site, „Molecular Biology of the Cell”, 6 (8), 1995, s. 1061–1075, DOI: 10.1091/mbc.6.8.1061, PMID: 7579708, PMCID: PMC301263 (ang.).
↑ R.R. Gary R.R., A.A. Bretscher A.A., Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins, „Proceedings of the National Academy of Sciences of the United States of America”, 90 (22), 1993, s. 10846–10850, DOI: 10.1073/pnas.90.22.10846, PMID: 8248180, PMCID: PMC47875 (ang.).
↑ O.M.O.M. Mykkänen O.M.O.M., M.M. Grönholm M.M., M.M. Rönty M.M., M.M. Lalowski M.M., P.P. Salmikangas P.P., Characterization of human palladin, a microfilament-associated protein, „Molecular Biology of the Cell”, 12 (10), 2001, s. 3060–3073, DOI: 10.1091/mbc.12.10.3060, PMID: 11598191, PMCID: PMC60155 (ang.).
↑ A.A. Gautreau A.A., P.P. Poullet P.P., D.D. Louvard D.D., M.M. Arpin M.M., Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway, „Proceedings of the National Academy of Sciences of the United States of America”, 96 (13), 1999, s. 7300–7305, DOI: 10.1073/pnas.96.13.7300, PMID: 10377409, PMCID: PMC22080 (ang.).

Przeczytaj ostrzeżenie dotyczące informacji medycznych i pokrewnych zamieszczonych w Wikipedii.

[1] William JamesW.J. Smith William JamesW.J., NicolasN. Nassar NicolasN., AnthonyA. Bretscher AnthonyA., Richard A.R.A. Cerione Richard A.R.A., P. AndrewP.A. Karplus P. AndrewP.A., Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions, „Journal of Biological Chemistry”, 278 (7), 2003, s. 4949–4956, DOI: 10.1074/jbc.M210601200, PMID: 12429733 (ang.).

[2] EZR [online], NCBI [dostęp 2020-03-29] (ang.).

[3] AgnieszkaA. Hałoń AgnieszkaA., PiotrP. Donizy PiotrP., Rodzina białek ERM (ezrin/radixin/moesin) – rola i znaczenie w procesach polaryzacji, adhezji i mobilności komórkowej, „Postepy Higieny I Medycyny Doswiadczalnej”, 66, 2012, s. 158–164, DOI: 10.5604/17322693.987628, PMID: 22470191 .

[pmid9748260-4] C.H.C.H. Yun C.H.C.H., G.G. Lamprecht G.G., D.V.D.V. Forster D.V.D.V., A.A. Sidor A.A., NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na⁺/H⁺ exchanger NHE3 and the cytoskeletal protein ezrin, „Journal of Biological Chemistry”, 273 (40), 1998, s. 25856–25863, DOI: 10.1074/jbc.273.40.25856, PMID: 9748260 (ang.).

[pmid12080047-5] Shanthi V.S.V. Sitaraman Shanthi V.S.V., LixinL. Wang LixinL., MichelleM. Wong MichelleM., MatthiasM. Bruewer MatthiasM., MichaelM. Hobert MichaelM., The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and Ezrin upon agonist stimulation, „Journal of Biological Chemistry”, 277 (36), 2002, s. 33188–33195, DOI: 10.1074/jbc.M202522200, PMID: 12080047 (ang.).

[pmid10036239-6] M.M. Grönholm M.M., M.M. Sainio M.M., F.F. Zhao F.F., L.L. Heiska L.L., A.A. Vaheri A.A., Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin, „Journal of Cell Science”, 112 (6), 1999, s. 895–904, PMID: 10036239 (ang.).

[pmid10704377-7] F.F. Granés F.F., J.M.J.M. Urena J.M.J.M., N.N. Rocamora N.N., S.S. Vilaró S.S., Ezrin links syndecan-2 to the cytoskeleton, „Journal of Cell Science”, 113 (7), 2000, s. 1267–1276, PMID: 10704377 (ang.).

[pmid9616160-8] J.M.J.M. Serrador J.M.J.M., M.M. Nieto M.M., J.L.J.L. Alonso-Lebrero J.L.J.L., M.A. delM.A. Pozo M.A. delM.A., J.J. Calvo J.J., CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts, „Blood”, 91 (12), 1998, s. 4632–4644, DOI: 10.1182/blood.V91.12.4632, PMID: 9616160 (ang.).

[pmid15659383-9] 1 2 ConsueloC. Gajate ConsueloC., FaustinoF. Mollinedo FaustinoF., Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy, „Journal of Biological Chemistry”, 280 (12), 2005, s. 11641–11647, DOI: 10.1074/jbc.M411781200, PMID: 15659383 (ang.).

[pmid11013215-10] S.S. Parlato S.S., A.M.A.M. Giammarioli A.M.A.M., M.M. Logozzi M.M., F.F. Lozupone F.F., P.P. Matarrese P.P., CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway, „The EMBO Journal”, 19 (19), 2000, s. 5123–5134, DOI: 10.1093/emboj/19.19.5123, PMID: 11013215, PMCID: PMC302100 (ang.).

[pmid12082081-11] OlgaO. Barreiro OlgaO., MariaM. Yanez-Mo MariaM., Juan M.J.M. Serrador Juan M.J.M., Maria C.M.C. Montoya Maria C.M.C., MiguelM. Vicente-Manzanares MiguelM., Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes, „The Journal of Cell Biology”, 157 (7), 2002, s. 1233–1245, DOI: 10.1083/jcb.200112126, PMID: 12082081, PMCID: PMC2173557 (ang.).

[pmid12808036-12] MaxM. Koltzscher MaxM., ClaudiaC. Neumann ClaudiaC., SimoneS. König SimoneS., VolkerV. Gerke VolkerV., Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P, „Molecular Biology of the Cell”, 14 (6), 2003, s. 2372–2384, DOI: 10.1091/mbc.e02-09-0553, PMID: 12808036, PMCID: PMC194886 (ang.).

[pmid9705328-13] 1 2 3 L.L. Heiska L.L., K.K. Alfthan K.K., M.M. Grönholm M.M., P.P. Vilja P.P., A.A. Vaheri A.A., Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate, „Journal of Biological Chemistry”, 273 (34), 1998, s. 21893–21900, DOI: 10.1074/jbc.273.34.21893, PMID: 9705328 (ang.).

[pmid11784723-14] Juan M.J.M. Serrador Juan M.J.M., MiguelM. Vicente-Manzanares MiguelM., JavierJ. Calvo JavierJ., OlgaO. Barreiro OlgaO., Maria C.M.C. Montoya Maria C.M.C., A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting, „Journal of Biological Chemistry”, 277 (12), 2002, s. 10400–10409, DOI: 10.1074/jbc.M110694200, PMID: 11784723 (ang.).

[pmid11684085-15] N.N. Brdicková N.N., T.T. Brdicka T.T., L.L. Andera L.L., J.J. Spicka J.J., P.P. Angelisová P.P., Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton, „FEBS Letters”, 507 (2), 2001, s. 133–136, DOI: 10.1016/s0014-5793(01)02955-6, PMID: 11684085 (ang.).

[pmid9314537-16] D.D. Reczek D.D., M.M. Berryman M.M., A.A. Bretscher A.A., Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family, „The Journal of Cell Biology”, 139 (1), 1997, s. 169–179, DOI: 10.1083/jcb.139.1.169, PMID: 9314537, PMCID: PMC2139813 (ang.).

[pmid7579708-17] R.R. Gary R.R., A.A. Bretscher A.A., Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site, „Molecular Biology of the Cell”, 6 (8), 1995, s. 1061–1075, DOI: 10.1091/mbc.6.8.1061, PMID: 7579708, PMCID: PMC301263 (ang.).

[pmid8248180-18] R.R. Gary R.R., A.A. Bretscher A.A., Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins, „Proceedings of the National Academy of Sciences of the United States of America”, 90 (22), 1993, s. 10846–10850, DOI: 10.1073/pnas.90.22.10846, PMID: 8248180, PMCID: PMC47875 (ang.).

[pmid11598191-19] O.M.O.M. Mykkänen O.M.O.M., M.M. Grönholm M.M., M.M. Rönty M.M., M.M. Lalowski M.M., P.P. Salmikangas P.P., Characterization of human palladin, a microfilament-associated protein, „Molecular Biology of the Cell”, 12 (10), 2001, s. 3060–3073, DOI: 10.1091/mbc.12.10.3060, PMID: 11598191, PMCID: PMC60155 (ang.).

[pmid10377409-20] A.A. Gautreau A.A., P.P. Poullet P.P., D.D. Louvard D.D., M.M. Arpin M.M., Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway, „Proceedings of the National Academy of Sciences of the United States of America”, 96 (13), 1999, s. 7300–7305, DOI: 10.1073/pnas.96.13.7300, PMID: 10377409, PMCID: PMC22080 (ang.).