Structure and Functions: ERM Protein Family

Divine Mensah Sedzro; Sm Faysal Bellah; Hameed Akbar; Sardar Mohammad Saker Billah

doi:doi:10.11648/j.cb.20180602.11

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Structure and Functions: ERM Protein Family

Divine Mensah Sedzro, Sm Faysal Bellah, Hameed Akbar, Sardar Mohammad Saker Billah

Published in Cell Biology (Volume 6, Issue 2)

Received: 15 September 2018 Accepted: 6 October 2018 Published: 29 October 2018

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Abstract

Preservation of the structural integrity of the cell depends on the plasma membrane in eukaryotic cells. Interaction between plasma membrane, cytoskeleton and proper anchorage influence regular cellular processes. The needed regulated connection between the membrane and the underlying actin cytoskeleton is therefore made available by the ERM (Ezrin, Radixin, and Moesin) family of proteins. ERM proteins also afford the required environment for the diffusion of signals in reactions to extracellular signals. Other studies have confirmed the importance of ERM proteins in different mode organisms and in cultured cells to emphasize the generation and maintenance of specific domains of the plasma membrane. An essential attribute of almost all cells are the specialized membrane domains. They are specifically important to tissues like the intestinal brush border epithelium, with a highly organized cell cortex including a compound array of apical microvilli, an apical junctional complex, and a basolateral membrane domain. This paper critically looks at the structure and functions of the ERM proteins and briefly presents the activation and deactivation mechanism through careful analysis on works done on this protein and its prospects. It is obvious from the discussion presented in this paper that the ERM (Ezrin, Radixin, and Moesin) proteins play very vital roles in mediating signal transduction and maintaining cellular integrity from a variety of extracellular inputs through their interaction with different receptor tyrosine kinases (RTKs) such as EGFR and HGFR, adhesion and adaptor proteins such as E-cadherin, ICAM-1,2,3, NHERF and CD44, and other signaling pathways such as PI3K/Akt, cAMP/PKA and the Rho GTPases, all of which have been implicated in tumorigenesis; thus, making ERM proteins a crucial target in development of novel therapeutics in fighting cancer progression and other related disease conditions where the protein is implicated. Further analysis on the structure and reaction mechanism of this protein is needed to exploit its full potential for clinical and other uses.

Published in	Cell Biology (Volume 6, Issue 2)
DOI	10.11648/j.cb.20180602.11
Page(s)	20-32
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2018. Published by Science Publishing Group

Keywords

Cytoskeleton, Ezrin, Radixin, Moesin, Basolateral, Membrane, Domain

References

[1]	Edwards, S. D. and N. H. Keep, The 2.7 Å crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation. Biochemistry, 2001. 40(24): p. 7061-7068.
[2]	Lopez, E. W., et al., The ERM family member Merlin is required for endometrial gland morphogenesis. Developmental biology, 2018. 442(2): p. 301-314.
[3]	Solinet, S., et al., The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex. J Cell Biol, 2013: p. jcb. 201304052.
[4]	Chirivino, D., et al., The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes. Molecular biology of the cell, 2011. 22(3): p. 375-385.
[5]	Bretscher, A., Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. The Journal of Cell Biology, 1983. 97(2): p. 425-432.
[6]	Tsukita, S. and Y. Hieda, A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization. The Journal of cell biology, 1989. 108(6): p. 2369-2382.
[7]	Kschonsak, Y. T. and I. Hoffmann, Activated ezrin controls MISP levels to ensure correct NuMA polarization and spindle orientation. J Cell Sci, 2018: p. jcs. 214544.
[8]	Lankes, W., et al., A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation. Biochemical Journal, 1988. 251(3): p. 831-842.
[9]	Satooka, H., et al., The ERM Protein Moesin Regulates CD8+ Regulatory T Cell Homeostasis and Self-Tolerance. The Journal of Immunology, 2017: p. ji1700074.
[10]	Yonemura, S., et al., Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. The Journal of cell biology, 1998. 140(4): p. 885-895.
[11]	Hamada, K., et al., Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin—ICAM-2 complex. The EMBO journal, 2003. 22(3): p. 502-514.
[12]	Tsukita, S., S. Yonemura, and S. Tsukita, ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends in biochemical sciences, 1997. 22(2): p. 53-58.
[13]	Bretscher, A., K. Edwards, and R. G. Fehon, ERM proteins and merlin: integrators at the cell cortex. Nature reviews Molecular cell biology, 2002. 3(8): p. 586-599.
[14]	Fiévet, B., D. Louvard, and M. Arpin, ERM proteins in epithelial cell organization and functions. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 2007. 1773(5): p. 653-660.
[15]	Sato, N., et al., A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. Journal of Cell Science, 1992. 103(1): p. 131-143.
[16]	van Furden, D., et al., The C. elegans ezrin-radixin-moesin protein ERM-1 is necessary for apical junction remodelling and tubulogenesis in the intestine. Developmental biology, 2004. 272(1): p. 262-276.
[17]	Smith, W. J., et al., Structure of the Active N-terminal Domain of Ezrin CONFORMATIONAL AND MOBILITY CHANGES IDENTIFY KEYSTONE INTERACTIONS. Journal of Biological Chemistry, 2003. 278(7): p. 4949-4956.
[18]	Pearson, M. A., et al., Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell, 2000. 101(3): p. 259-270.
[19]	Li, Q., et al., Self-masking in an intact ERM-merlin protein: an active role for the central α-helical domain. Journal of molecular biology, 2007. 365(5): p. 1446-1459.
[20]	Hlavaty, J., et al., Ezrin and moesin expression in canine and feline osteosarcoma. Histology and histopathology, 2017. 32(8): p. 805-816.
[21]	Hirao, M., et al., Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. The Journal of cell biology, 1996. 135(1): p. 37-51.
[22]	Shabardina, V., et al., Mode of ezrin-membrane interaction as a function of PIP2 binding and pseudophosphorylation. Biophysical journal, 2016. 110(12): p. 2710-2719.
[23]	Yonemura, S., et al., Rho-dependent and-independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo. Journal of cell science, 2002. 115(12): p. 2569-2580.
[24]	Fievet, B. T., et al., Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin. The Journal of cell biology, 2004. 164(5): p. 653-659.
[25]	Göbel, V., et al., Lumen morphogenesis in C. elegans requires the membrane-cytoskeleton linker erm-1. Developmental cell, 2004. 6(6): p. 865-873.
[26]	Biri-Kovács, B., et al., Ezrin interacts with S100A4 via both its N-and C-terminal domains. PloS one, 2017. 12(5): p. e0177489.
[27]	Nakamura, F., M. R. Amieva, and H. Furthmayr, Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets. Journal of Biological Chemistry, 1995. 270(52): p. 31377-31385.
[28]	Pietromonaco, S. F., et al., Protein kinase C-θ phosphorylation of moesin in the actin-binding sequence. Journal of Biological Chemistry, 1998. 273(13): p. 7594-7603.
[29]	Pilot, F., et al., Spatial control of actin organization at adherens junctions by a synaptotagmin-like protein. Nature, 2006. 442(7102): p. 580-584.
[30]	Ng, T., et al., Ezrin is a downstream effector of trafficking PKC–integrin complexes involved in the control of cell motility. The EMBO journal, 2001. 20(11): p. 2723-2741.
[31]	Baumgartner, M., et al., The Nck-interacting kinase phosphorylates ERM proteins for formation of lamellipodium by growth factors. Proceedings of the National Academy of Sciences, 2006. 103(36): p. 13391-13396.
[32]	Fehon, R. G., A. I. McClatchey, and A. Bretscher, Organizing the cell cortex: the role of ERM proteins. Nature reviews Molecular cell biology, 2010. 11(4): p. 276-287.
[33]	Arpin, M., et al., Emerging role for ERM proteins in cell adhesion and migration. Cell adhesion & migration, 2011. 5(2): p. 199-206.
[34]	Yano, K., et al., Different regulation of P-glycoprotein function between Caco-2 and Caki-1 cells by ezrin, radixin and moesin proteins. Journal of Pharmacy and Pharmacology, 2016. 68(3): p. 361-367.
[35]	Wakayama, T., et al., Expression, localization, and binding activity of the ezrin/radixin/moesin proteins in the mouse testis. Journal of Histochemistry & Cytochemistry, 2009. 57(4): p. 351-362.
[36]	Pore, D. and N. Gupta, The ezrin-radixin-moesin family of proteins in the regulation of B-cell immune response. Critical Reviews™ in Immunology, 2015. 35(1).
[37]	Nakamura, N., et al., Phosphorylation of ERM proteins at filopodia induced by Cdc42. Genes to Cells, 2000. 5(7): p. 571-581.
[38]	Mackay, D. J., et al., Rho-and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. The Journal of cell biology, 1997. 138(4): p. 927-938.
[39]	Belkina, N. V., et al., LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation. Proceedings of the National Academy of Sciences, 2009. 106(12): p. 4707-4712.
[40]	Bretscher, A., Regulation of cortical structure by the ezrin-radixin-moesin protein family. Current opinion in cell biology, 1999. 11(1): p. 109-116.
[41]	Shaw, R. J., et al., RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Molecular biology of the cell, 1998. 9(2): p. 403-419.
[42]	Wangkahart, E., C. J. Secombes, and T. Wang, Dissecting the immune pathways stimulated following injection vaccination of rainbow trout (Oncorhynchus mykiss) against enteric redmouth disease (ERM). Fish & shellfish immunology, 2017.
[43]	Ivetic, A. and A. J. Ridley, Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes. Immunology, 2004. 112(2): p. 165-176.
[44]	Krieg, J. and T. Hunter, Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin. Journal of Biological Chemistry, 1992. 267(27): p. 19258-19265.
[45]	Gautreau, A., et al., Ezrin, a plasma membrane–microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway. Proceedings of the National Academy of Sciences, 1999. 96(13): p. 7300-7305.
[46]	Adada, M., et al., Sphingolipid regulation of ezrin, radixin, and moesin proteins family: implications for cell dynamics. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 2014. 1841(5): p. 727-737.
[47]	Adyshev, D. M., et al., Differential involvement of ezrin/radixin/moesin proteins in sphingosine 1-phosphate-induced human pulmonary endothelial cell barrier enhancement. Cellular signalling, 2011. 23(12): p. 2086-2096.
[48]	Adyshev, D. M., et al., Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin. American Journal of Physiology-Lung Cellular and Molecular Physiology, 2013. 305(3): p. L240-L255.
[49]	Bakolitsa, C., et al., Crystal structure of the vinculin tail suggests a pathway for activation. Cell, 1999. 99(6): p. 603-613.
[50]	Berryman, M., Z. Franck, and A. Bretscher, Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. Journal of cell science, 1993. 105(4): p. 1025-1043.
[51]	Ponuwei, G. A., A glimpse of the ERM proteins. Journal of biomedical science, 2016. 23(1): p. 35.
[52]	Borg, J. and B. Margolis, Function of PTB domains, in Protein Modules in Signal Transduction. 1998, Springer. p. 23-38.
[53]	Chishti, A. H., et al., The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane. Trends in biochemical sciences, 1998. 23(8): p. 281-282.
[54]	Turunen, J. and F. Wyrowski, Diffractive optics for industrial and commercial applications. Diffractive Optics for Industrial and Commercial Applications, by Jari Turunen (Editor), Frank Wyrowski (Editor), pp. 440. ISBN 3-527-40100-8. Wiley-VCH, March 1998., 1998: p. 440.
[55]	Doi, Y., et al., Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout. Journal of Biological Chemistry, 1999. 274(4): p. 2315-2321.
[56]	Dransfield, D. T., et al., Ezrin is a cyclic AMP-dependent protein kinase anchoring protein. The EMBO Journal, 1997. 16(1): p. 35-43.
[57]	Fedorov, A. A., et al., Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. Nature Structural & Molecular Biology, 1999. 6(7): p. 661-665.
[58]	Ferguson, K. M., et al., Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell, 1995. 83(6): p. 1037-1046.
[59]	Forman-Kay, J. D. and T. Pawson, Diversity in protein recognition by PTB domains. Current opinion in structural biology, 1999. 9(6): p. 690-695.
[60]	Furey, W. and S. Swaminathan, PHASES-95: A program package for processing and analyzing diffraction data from macromolecules. Methods in enzymology, 1997. 277: p. 590-620.
[61]	Gary, R. and A. Bretscher, 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, 1995. 6(8): p. 1061-1075.
[62]	Funayama, N., et al., Radixin is a novel member of the band 4.1 family. The Journal of Cell Biology, 1991. 115(4): p. 1039-1048.
[63]	Girault, J.-A., et al., Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction. Molecular Medicine, 1998. 4(12): p. 751.
[64]	Oshiro, N., Y. Fukata, and K. Kaibuchi, Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures. Journal of Biological Chemistry, 1998. 273(52): p. 34663-34666.
[65]	ten Klooster, J. P., et al., Mst4 and Ezrin induce brush borders downstream of the Lkb1/Strad/Mo25 polarization complex. Developmental cell, 2009. 16(4): p. 551-562.
[66]	Popoff, M. R. and B. Geny, Multifaceted role of Rho, Rac, Cdc42 and Ras in intercellular junctions, lessons from toxins. Biochimica et Biophysica Acta (BBA)-Biomembranes, 2009. 1788(4): p. 797-812.
[67]	Weinman, E. J., et al., The association of NHERF adaptor proteins with G protein–coupled receptors and receptor tyrosine kinases. Annu. Rev. Physiol., 2006. 68: p. 491-505.
[68]	Reczek, D., M. Berryman, and A. Bretscher, Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. The Journal of cell biology, 1997. 139(1): p. 169-179.
[69]	Asp, N., et al., Regulation of ErbB2 localization and function in breast cancer cells by ERM proteins. Oncotarget, 2016. 7(18): p. 25443.
[70]	Algrain, M., et al., Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. The Journal of cell biology, 1993. 120(1): p. 129-139.
[71]	Gould, K. L., et al., cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1. The EMBO journal, 1989. 8(13): p. 4133.
[72]	Farago, B., et al., Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy. Biophysical journal, 2010. 99(10): p. 3473-3482.
[73]	Jayasundar, J. J., et al., Open conformation of ezrin bound to phosphatidylinositol 4, 5-bisphosphate and to F-actin revealed by neutron scattering. Journal of Biological Chemistry, 2012. 287(44): p. 37119-37133.
[74]	Mohanraj, R., et al., Immunohistochemical expression of ezrin in oral potentially malignant disorders-A descriptive study. Journal of pharmacy & bioallied sciences, 2017. 9(Suppl 1): p. S205.
[75]	Serrador, J. M., et al., CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. Blood, 1998. 91(12): p. 4632-4644.
[76]	Gajate, C. and F. Mollinedo, Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy. Journal of Biological Chemistry, 2005. 280(12): p. 11641-11647.
[77]	Heiska, L., et al., 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, 1998. 273(34): p. 21893-21900.
[78]	Gronholm, M., et al., Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin. Journal of cell science, 1999. 112(6): p. 895-904.
[79]	Mykkänen, O.-M., et al., Characterization of human palladin, a microfilament-associated protein. Molecular biology of the cell, 2001. 12(10): p. 3060-3073.
[80]	Brdičková, N., et al., Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton. FEBS letters, 2001. 507(2): p. 133-136.
[81]	Yun, C.-H. C., et al., NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin. Journal of Biological Chemistry, 1998. 273(40): p. 25856-25863.
[82]	Sitaraman, S. V., et al., The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and Ezrin upon agonist stimulation. Journal of Biological Chemistry, 2002. 277(36): p. 33188-33195.
[83]	Barreiro, O., et al., 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, 2002. 157(7): p. 1233-1245.
[84]	Hoeflich, K. P. and M. Ikura, Radixin: cytoskeletal adopter and signaling protein. The international journal of biochemistry & cell biology, 2004. 36(11): p. 2131-2136.
[85]	Kikuchi, S., et al., Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. Nature genetics, 2002. 31(3): p. 320-325.
[86]	Dickson, T. C., et al., Functional binding interaction identified between the axonal CAM L1 and members of the ERM family. The Journal of cell biology, 2002. 157(7): p. 1105-1112.
[87]	Haddad, L. A., et al., The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton. Journal of Biological Chemistry, 2002. 277(46): p. 44180-44186.
[88]	Wientjes, F. B., et al., The NADPH oxidase components p47phox and p40phox bind to moesin through their PX domain. Biochemical and biophysical research communications, 2001. 289(2): p. 382-388.
[89]	Matsumoto, M. and T. Hirata, Moesin regulates neutrophil rolling velocity in vivo. Cellular immunology, 2016. 304: p. 59-62.
[90]	Wang, C. C., et al., Differential expression of moesin in breast cancers and its implication in epithelial–mesenchymal transition. Histopathology, 2012. 61(1): p. 78-87.
[91]	Abiatari, I., et al., Moesin-dependent cytoskeleton remodelling is associated with an anaplastic phenotype of pancreatic cancer. Journal of cellular and molecular medicine, 2010. 14(5): p. 1166-1179.
[92]	Charafe-Jauffret, E., et al., Moesin expression is a marker of basal breast carcinomas. International journal of cancer, 2007. 121(8): p. 1779-1785.

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Divine Mensah Sedzro, Sm Faysal Bellah, Hameed Akbar, Sardar Mohammad Saker Billah. (2018). Structure and Functions: ERM Protein Family. Cell Biology, 6(2), 20-32. https://doi.org/10.11648/j.cb.20180602.11

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ACS Style

Divine Mensah Sedzro; Sm Faysal Bellah; Hameed Akbar; Sardar Mohammad Saker Billah. Structure and Functions: ERM Protein Family. Cell Biol. 2018, 6(2), 20-32. doi: 10.11648/j.cb.20180602.11

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AMA Style

Divine Mensah Sedzro, Sm Faysal Bellah, Hameed Akbar, Sardar Mohammad Saker Billah. Structure and Functions: ERM Protein Family. Cell Biol. 2018;6(2):20-32. doi: 10.11648/j.cb.20180602.11

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@article{10.11648/j.cb.20180602.11,
  author = {Divine Mensah Sedzro and Sm Faysal Bellah and Hameed Akbar and Sardar Mohammad Saker Billah},
  title = {Structure and Functions: ERM Protein Family},
  journal = {Cell Biology},
  volume = {6},
  number = {2},
  pages = {20-32},
  doi = {10.11648/j.cb.20180602.11},
  url = {https://doi.org/10.11648/j.cb.20180602.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.cb.20180602.11},
  abstract = {Preservation of the structural integrity of the cell depends on the plasma membrane in eukaryotic cells. Interaction between plasma membrane, cytoskeleton and proper anchorage influence regular cellular processes. The needed regulated connection between the membrane and the underlying actin cytoskeleton is therefore made available by the ERM (Ezrin, Radixin, and Moesin) family of proteins. ERM proteins also afford the required environment for the diffusion of signals in reactions to extracellular signals. Other studies have confirmed the importance of ERM proteins in different mode organisms and in cultured cells to emphasize the generation and maintenance of specific domains of the plasma membrane. An essential attribute of almost all cells are the specialized membrane domains. They are specifically important to tissues like the intestinal brush border epithelium, with a highly organized cell cortex including a compound array of apical microvilli, an apical junctional complex, and a basolateral membrane domain. This paper critically looks at the structure and functions of the ERM proteins and briefly presents the activation and deactivation mechanism through careful analysis on works done on this protein and its prospects. It is obvious from the discussion presented in this paper that the ERM (Ezrin, Radixin, and Moesin) proteins play very vital roles in mediating signal transduction and maintaining cellular integrity from a variety of extracellular inputs through their interaction with different receptor tyrosine kinases (RTKs) such as EGFR and HGFR, adhesion and adaptor proteins such as E-cadherin, ICAM-1,2,3, NHERF and CD44, and other signaling pathways such as PI3K/Akt, cAMP/PKA and the Rho GTPases, all of which have been implicated in tumorigenesis; thus, making ERM proteins a crucial target in development of novel therapeutics in fighting cancer progression and other related disease conditions where the protein is implicated. Further analysis on the structure and reaction mechanism of this protein is needed to exploit its full potential for clinical and other uses.},
 year = {2018}
}

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TY  - JOUR
T1  - Structure and Functions: ERM Protein Family
AU  - Divine Mensah Sedzro
AU  - Sm Faysal Bellah
AU  - Hameed Akbar
AU  - Sardar Mohammad Saker Billah
Y1  - 2018/10/29
PY  - 2018
N1  - https://doi.org/10.11648/j.cb.20180602.11
DO  - 10.11648/j.cb.20180602.11
T2  - Cell Biology
JF  - Cell Biology
JO  - Cell Biology
SP  - 20
EP  - 32
PB  - Science Publishing Group
SN  - 2330-0183
UR  - https://doi.org/10.11648/j.cb.20180602.11
AB  - Preservation of the structural integrity of the cell depends on the plasma membrane in eukaryotic cells. Interaction between plasma membrane, cytoskeleton and proper anchorage influence regular cellular processes. The needed regulated connection between the membrane and the underlying actin cytoskeleton is therefore made available by the ERM (Ezrin, Radixin, and Moesin) family of proteins. ERM proteins also afford the required environment for the diffusion of signals in reactions to extracellular signals. Other studies have confirmed the importance of ERM proteins in different mode organisms and in cultured cells to emphasize the generation and maintenance of specific domains of the plasma membrane. An essential attribute of almost all cells are the specialized membrane domains. They are specifically important to tissues like the intestinal brush border epithelium, with a highly organized cell cortex including a compound array of apical microvilli, an apical junctional complex, and a basolateral membrane domain. This paper critically looks at the structure and functions of the ERM proteins and briefly presents the activation and deactivation mechanism through careful analysis on works done on this protein and its prospects. It is obvious from the discussion presented in this paper that the ERM (Ezrin, Radixin, and Moesin) proteins play very vital roles in mediating signal transduction and maintaining cellular integrity from a variety of extracellular inputs through their interaction with different receptor tyrosine kinases (RTKs) such as EGFR and HGFR, adhesion and adaptor proteins such as E-cadherin, ICAM-1,2,3, NHERF and CD44, and other signaling pathways such as PI3K/Akt, cAMP/PKA and the Rho GTPases, all of which have been implicated in tumorigenesis; thus, making ERM proteins a crucial target in development of novel therapeutics in fighting cancer progression and other related disease conditions where the protein is implicated. Further analysis on the structure and reaction mechanism of this protein is needed to exploit its full potential for clinical and other uses.
VL  - 6
IS  - 2
ER  -

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Author Information

Divine Mensah Sedzro

Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China
Sm Faysal Bellah

Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China
Hameed Akbar

Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China
Sardar Mohammad Saker Billah

Department of Chemistry, Govt. M. M. University College, Jessore, Bangladesh

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Divine Mensah Sedzro, Sm Faysal Bellah, Hameed Akbar, Sardar Mohammad Saker Billah. (2018). Structure and Functions: ERM Protein Family. Cell Biology, 6(2), 20-32. https://doi.org/10.11648/j.cb.20180602.11

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Divine Mensah Sedzro; Sm Faysal Bellah; Hameed Akbar; Sardar Mohammad Saker Billah. Structure and Functions: ERM Protein Family. Cell Biol. 2018, 6(2), 20-32. doi: 10.11648/j.cb.20180602.11

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AMA Style

Divine Mensah Sedzro, Sm Faysal Bellah, Hameed Akbar, Sardar Mohammad Saker Billah. Structure and Functions: ERM Protein Family. Cell Biol. 2018;6(2):20-32. doi: 10.11648/j.cb.20180602.11

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@article{10.11648/j.cb.20180602.11,
  author = {Divine Mensah Sedzro and Sm Faysal Bellah and Hameed Akbar and Sardar Mohammad Saker Billah},
  title = {Structure and Functions: ERM Protein Family},
  journal = {Cell Biology},
  volume = {6},
  number = {2},
  pages = {20-32},
  doi = {10.11648/j.cb.20180602.11},
  url = {https://doi.org/10.11648/j.cb.20180602.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.cb.20180602.11},
  abstract = {Preservation of the structural integrity of the cell depends on the plasma membrane in eukaryotic cells. Interaction between plasma membrane, cytoskeleton and proper anchorage influence regular cellular processes. The needed regulated connection between the membrane and the underlying actin cytoskeleton is therefore made available by the ERM (Ezrin, Radixin, and Moesin) family of proteins. ERM proteins also afford the required environment for the diffusion of signals in reactions to extracellular signals. Other studies have confirmed the importance of ERM proteins in different mode organisms and in cultured cells to emphasize the generation and maintenance of specific domains of the plasma membrane. An essential attribute of almost all cells are the specialized membrane domains. They are specifically important to tissues like the intestinal brush border epithelium, with a highly organized cell cortex including a compound array of apical microvilli, an apical junctional complex, and a basolateral membrane domain. This paper critically looks at the structure and functions of the ERM proteins and briefly presents the activation and deactivation mechanism through careful analysis on works done on this protein and its prospects. It is obvious from the discussion presented in this paper that the ERM (Ezrin, Radixin, and Moesin) proteins play very vital roles in mediating signal transduction and maintaining cellular integrity from a variety of extracellular inputs through their interaction with different receptor tyrosine kinases (RTKs) such as EGFR and HGFR, adhesion and adaptor proteins such as E-cadherin, ICAM-1,2,3, NHERF and CD44, and other signaling pathways such as PI3K/Akt, cAMP/PKA and the Rho GTPases, all of which have been implicated in tumorigenesis; thus, making ERM proteins a crucial target in development of novel therapeutics in fighting cancer progression and other related disease conditions where the protein is implicated. Further analysis on the structure and reaction mechanism of this protein is needed to exploit its full potential for clinical and other uses.},
 year = {2018}
}

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TY  - JOUR
T1  - Structure and Functions: ERM Protein Family
AU  - Divine Mensah Sedzro
AU  - Sm Faysal Bellah
AU  - Hameed Akbar
AU  - Sardar Mohammad Saker Billah
Y1  - 2018/10/29
PY  - 2018
N1  - https://doi.org/10.11648/j.cb.20180602.11
DO  - 10.11648/j.cb.20180602.11
T2  - Cell Biology
JF  - Cell Biology
JO  - Cell Biology
SP  - 20
EP  - 32
PB  - Science Publishing Group
SN  - 2330-0183
UR  - https://doi.org/10.11648/j.cb.20180602.11
AB  - Preservation of the structural integrity of the cell depends on the plasma membrane in eukaryotic cells. Interaction between plasma membrane, cytoskeleton and proper anchorage influence regular cellular processes. The needed regulated connection between the membrane and the underlying actin cytoskeleton is therefore made available by the ERM (Ezrin, Radixin, and Moesin) family of proteins. ERM proteins also afford the required environment for the diffusion of signals in reactions to extracellular signals. Other studies have confirmed the importance of ERM proteins in different mode organisms and in cultured cells to emphasize the generation and maintenance of specific domains of the plasma membrane. An essential attribute of almost all cells are the specialized membrane domains. They are specifically important to tissues like the intestinal brush border epithelium, with a highly organized cell cortex including a compound array of apical microvilli, an apical junctional complex, and a basolateral membrane domain. This paper critically looks at the structure and functions of the ERM proteins and briefly presents the activation and deactivation mechanism through careful analysis on works done on this protein and its prospects. It is obvious from the discussion presented in this paper that the ERM (Ezrin, Radixin, and Moesin) proteins play very vital roles in mediating signal transduction and maintaining cellular integrity from a variety of extracellular inputs through their interaction with different receptor tyrosine kinases (RTKs) such as EGFR and HGFR, adhesion and adaptor proteins such as E-cadherin, ICAM-1,2,3, NHERF and CD44, and other signaling pathways such as PI3K/Akt, cAMP/PKA and the Rho GTPases, all of which have been implicated in tumorigenesis; thus, making ERM proteins a crucial target in development of novel therapeutics in fighting cancer progression and other related disease conditions where the protein is implicated. Further analysis on the structure and reaction mechanism of this protein is needed to exploit its full potential for clinical and other uses.
VL  - 6
IS  - 2
ER  -

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