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Journal articles on the topic 'ERM PROTEINS'

Author: Grafiati

Published: 14 March 2023

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1

McClatchey, Andrea I. "ERM proteins." Current Biology 22, no. 18 (2012): R784—R785. http://dx.doi.org/10.1016/j.cub.2012.07.057.

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McClatchey, Andrea I. "ERM proteins at a glance." Journal of Cell Science 127, no. 15 (2014): 3199–204. http://dx.doi.org/10.1242/jcs.098343.

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Clucas, J., and F. Valderrama. "ERM proteins in cancer progression." Journal of Cell Science 127, no. 2 (2014): 267–75. http://dx.doi.org/10.1242/jcs.133108.

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Clucas, J., and F. Valderrama. "ERM proteins in cancer progression." Journal of Cell Science 128, no. 6 (2015): 1253. http://dx.doi.org/10.1242/jcs.170027.

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5

Bagchi, M., M. Katar, W. K. Lo, R. Yost, C. Hill, and H. Maisel. "ERM proteins of the lens." Journal of Cellular Biochemistry 92, no. 3 (2004): 626–30. http://dx.doi.org/10.1002/jcb.20062.

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6

Kondo, Takahisa, Kosei Takeuchi, Yoshinori Doi, et al. "ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis." Journal of Cell Biology 139, no. 3 (1997): 749–58. http://dx.doi.org/10.1083/jcb.139.3.749.

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Breakdown of microvilli is a common early event in various types of apoptosis, but its molecular mechanism and implications remain unclear. ERM (ezrin/radixin/moesin) proteins are ubiquitously expressed microvillar proteins that are activated in the cytoplasm, translocate to the plasma membrane, and function as general actin filament/plasma membrane cross-linkers to form microvilli. Immunofluorescence microscopic and biochemical analyses revealed that, at the early phase of Fas ligand (FasL)–induced apoptosis in L cells expressing Fas (LHF), ERM proteins translocate from the plasma membranes o

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Yonemura, Shigenobu, Takeshi Matsui, Shoichiro Tsukita, and Sachiko Tsukita. "Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo." Journal of Cell Science 115, no. 12 (2002): 2569–80. http://dx.doi.org/10.1242/jcs.115.12.2569.

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Ezrin/radixin/moesin (ERM) proteins crosslink actin filaments to plasma membranes and are involved in the organization of the cortical cytoskeleton,especially in the formation of microvilli. ERM proteins are reported to be activated as crosslinkers in a Rho-dependent manner and are stabilized when phosphorylated at their C-terminal threonine residue to create C-terminal threonine-phosphorylated ERM proteins (CPERMs). Using a CPERM-specific mAb, we have shown, in vivo, that treatment with C3 transferase (a Rho inactivator) or staurosporine (a protein kinase inhibitor) leads to the dephosphoryla

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8

Hirao, M., N. Sato, T. Kondo, et al. "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway." Journal of Cell Biology 135, no. 1 (1996): 37–51. http://dx.doi.org/10.1083/jcb.135.1.37.

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The ERM proteins, ezrin, radixin, and moesin, are involved in the actin filament/plasma membrane interaction as cross-linkers. CD44 has been identified as one of the major membrane binding partners for ERM proteins. To examine the CD44/ERM protein interaction in vitro, we produced mouse ezrin, radixin, moesin, and the glutathione-S-transferase (GST)/CD44 cytoplasmic domain fusion protein (GST-CD44cyt) by means of recombinant baculovirus infection, and constructed an in vitro assay for the binding between ERM proteins and the cytoplasmic domain of CD44. In this system, ERM proteins bound to GST

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Yonemura, Shigenobu, Sachiko Tsukita, and Shoichiro Tsukita. "Direct Involvement of Ezrin/Radixin/Moesin (ERM)-binding Membrane Proteins in the Organization of Microvilli in Collaboration with Activated ERM Proteins." Journal of Cell Biology 145, no. 7 (1999): 1497–509. http://dx.doi.org/10.1083/jcb.145.7.1497.

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Ezrin/radixin/moesin (ERM) proteins have been thought to play a central role in the organization of cortical actin-based cytoskeletons including microvillar formation through cross-linking actin filaments and integral membrane proteins such as CD43, CD44, and ICAM-2. To examine the functions of these ERM-binding membrane proteins (ERMBMPs) in cortical morphogenesis, we overexpressed ERMBMPs (the extracellular domain of E-cadherin fused with the transmembrane/cytoplasmic domain of CD43, CD44, or ICAM-2) in various cultured cells. In cultured fibroblasts such as L and CV-1 cells, their overexpre

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Michie, Katharine A., Adam Bermeister, Neil O. Robertson, Sophia C. Goodchild, and Paul M. G. Curmi. "Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition." International Journal of Molecular Sciences 20, no. 8 (2019): 1996. http://dx.doi.org/10.3390/ijms20081996.

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The merlin-ERM (ezrin, radixin, moesin) family of proteins plays a central role in linking the cellular membranes to the cortical actin cytoskeleton. Merlin regulates contact inhibition and is an integral part of cell–cell junctions, while ERM proteins, ezrin, radixin and moesin, assist in the formation and maintenance of specialized plasma membrane structures and membrane vesicle structures. These two protein families share a common evolutionary history, having arisen and separated via gene duplication near the origin of metazoa. During approximately 0.5 billion years of evolution, the merlin

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11

Adyshev, Djanybek M., Steven M. Dudek, Nurgul Moldobaeva, et al. "Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin." American Journal of Physiology-Lung Cellular and Molecular Physiology 305, no. 3 (2013): L240—L255. http://dx.doi.org/10.1152/ajplung.00355.2012.

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Endothelial cell (EC) barrier disruption induced by inflammatory agonists such as thrombin leads to potentially lethal physiological dysfunction such as alveolar flooding, hypoxemia, and pulmonary edema. Thrombin stimulates paracellular gap and F-actin stress fiber formation, triggers actomyosin contraction, and alters EC permeability through multiple mechanisms that include protein kinase C (PKC) activation. We previously have shown that the ezrin, radixin, and moesin (ERM) actin-binding proteins differentially participate in sphingosine-1 phosphate-induced EC barrier enhancement. Phosphoryla

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Tavasoli, Mahtab, Abass Al-Momany, Xin Wang, Laiji Li, John C. Edwards, and Barbara J. Ballermann. "Both CLIC4 and CLIC5A activate ERM proteins in glomerular endothelium." American Journal of Physiology-Renal Physiology 311, no. 5 (2016): F945—F957. http://dx.doi.org/10.1152/ajprenal.00353.2016.

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The chloride intracellular channel (CLIC) 5A is expressed at very high levels in renal glomeruli, in both endothelial cells (EC) and podocytes. CLIC5A stimulates Rac1- and phosphatidylinositol (4,5)-bisphosphate-dependent ERM (ezrin, radixin, moesin) activation. ERM proteins, in turn, function in lumen formation and in the development of actin-based cellular projections. In mice lacking CLIC5A, ERM phosphorylation is profoundly reduced in podocytes, but preserved in glomerular EC. Since glomerular EC also express CLIC4, we reasoned that, if CLIC4 activates ERM proteins like CLIC5A, then CLIC4

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Chen, Emily, Meredith Shaffer, Verena Niggli, and Janis Burkhardt. "Flotillins and ERM proteins function to promote uropod formation in T cells (44.10)." Journal of Immunology 184, no. 1_Supplement (2010): 44.10. http://dx.doi.org/10.4049/jimmunol.184.supp.44.10.

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Abstract Migrating and adherent T cells form a protruding leading edge and a constricted tail-like structure termed the uropod. The formation of these two structures involves the segregation of specific cytoskeletal elements and cell surface molecules, including proteins that organize cell polarity in other systems. Among the proteins that are segregated to the uropod are ezrin and moesin, ERM family proteins that organize cell membrane domains by linking cytoplasmic and cytosolic proteins to the actin cytoskeleton. Using conditional ezrin-deficient mice in conjunction with siRNA for moesin, w

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Robertson, Tanner Ford, Daniel Blumenthal, Vidhi Chandra, and Janis K. Burkhardt. "ERM family proteins regulate T cell signal initiation by limiting Lck activity and T cell receptor clustering." Journal of Immunology 198, no. 1_Supplement (2017): 136.6. http://dx.doi.org/10.4049/jimmunol.198.supp.136.6.

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Abstract Ezrin, radixin, and moesin (ERM) proteins create specialized membrane subdomains by linking phosphatidyl inositol lipids and protein binding partners in the plasma membrane to the underlying actin cortex. These proteins are widely expressed and have well-characterized roles in cell polarity, development, and cytokinesis. In recent years, it has become clear that these proteins are also intimately involved in signal transduction. In humans, mutations in ERM proteins cause severe immunodeficiency characterized by lymphopenia and poor T cell proliferation. To investigate the role of ERM

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Gloerich, Martijn, Bas Ponsioen, Marjolein J. Vliem, et al. "Spatial Regulation of Cyclic AMP-Epac1 Signaling in Cell Adhesion by ERM Proteins." Molecular and Cellular Biology 30, no. 22 (2010): 5421–31. http://dx.doi.org/10.1128/mcb.00463-10.

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ABSTRACT Epac1 is a guanine nucleotide exchange factor for the small G protein Rap and is involved in membrane-localized processes such as integrin-mediated cell adhesion and cell-cell junction formation. Cyclic AMP (cAMP) directly activates Epac1 by release of autoinhibition and in addition induces its translocation to the plasma membrane. Here, we show an additional mechanism of Epac1 recruitment, mediated by activated ezrin-radixin-moesin (ERM) proteins. Epac1 directly binds with its N-terminal 49 amino acids to ERM proteins in their open conformation. Receptor-induced activation of ERM pro

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Hao, Jian-Jiang, Yin Liu, Michael Kruhlak, Karen E. Debell, Barbara L. Rellahan, and Stephen Shaw. "Phospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane." Journal of Cell Biology 184, no. 3 (2009): 451–62. http://dx.doi.org/10.1083/jcb.200807047.

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Mechanisms controlling the disassembly of ezrin/radixin/moesin (ERM) proteins, which link the cytoskeleton to the plasma membrane, are incompletely understood. In lymphocytes, chemokine (e.g., SDF-1) stimulation inactivates ERM proteins, causing their release from the plasma membrane and dephosphorylation. SDF-1–mediated inactivation of ERM proteins is blocked by phospholipase C (PLC) inhibitors. Conversely, reduction of phosphatidylinositol 4,5-bisphosphate (PIP2) levels by activation of PLC, expression of active PLC mutants, or acute targeting of phosphoinositide 5-phosphatase to the plasma

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17

Lopez, James P., Jerrold R. Turner, and Louis H. Philipson. "Glucose-induced ERM protein activation and translocation regulates insulin secretion." American Journal of Physiology-Endocrinology and Metabolism 299, no. 5 (2010): E772—E785. http://dx.doi.org/10.1152/ajpendo.00199.2010.

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A key step in regulating insulin secretion is insulin granule trafficking to the plasma membrane. Using live-cell time-lapse confocal microscopy, we observed a dynamic association of insulin granules with filamentous actin and PIP2-enriched structures. We found that the scaffolding protein family ERM, comprising ezrin, radixin, and moesin, are expressed in β-cells and target both F-actin and PIP2. Furthermore, ERM proteins are activated via phosphorylation in a glucose- and calcium-dependent manner. This activation leads to a translocation of the ERM proteins to sites on the cell periphery enr

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18

Gandy, K. Alexa Orr, Daniel Canals, Mohamad Adada, et al. "Sphingosine 1-phosphate induces filopodia formation through S1PR2 activation of ERM proteins." Biochemical Journal 449, no. 3 (2013): 661–72. http://dx.doi.org/10.1042/bj20120213.

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Previously we demonstrated that the sphingolipids ceramide and S1P (sphingosine 1-phosphate) regulate phosphorylation of the ERM (ezrin/radixin/moesin) family of cytoskeletal proteins [Canals, Jenkins, Roddy, Hernande-Corbacho, Obeid and Hannun (2010) J. Biol. Chem. 285, 32476–3285]. In the present article, we show that exogenously applied or endogenously generated S1P (in a sphingosine kinase-dependent manner) results in significant increases in phosphorylation of ERM proteins as well as filopodia formation. Using phosphomimetic and non-phosphorylatable ezrin mutants, we show that the S1P-ind

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Yang, Hai-Su, Kamilah Alexander, Pedro Santiago, and Philip W. Hinds. "ERM Proteins and Cdk5 in Cellular Senescence." Cell Cycle 2, no. 6 (2003): 517–20. http://dx.doi.org/10.4161/cc.2.6.582.

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Proudfit, Austin, Nabanita Bhunia, Debasis Pore, Yvonne Parker, Daniel Lindner, and Neetu Gupta. "Pharmacologic Inhibition of Ezrin-Radixin-Moesin Phosphorylation is a Novel Therapeutic Strategy in Rhabdomyosarcoma." Sarcoma 2020 (September 9, 2020): 1–11. http://dx.doi.org/10.1155/2020/9010496.

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Intermediate and high-risk rhabdomyosarcoma (RMS) patients have poor prognosis with available treatment options, highlighting a clear unmet need for identification of novel therapeutic strategies. Ezrin-radixin-moesin (ERM) family members are membrane-cytoskeleton linker proteins with well-defined roles in tumor metastasis, growth, and survival. ERM protein activity is regulated by dynamic changes in the phosphorylation at a conserved threonine residue in their C-terminal actin-binding domain. Interestingly, ERM family member, ezrin, has elevated expression in the RMS tissue. Despite this, the

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Ramalho, João J., Jorian J. Sepers, Ophélie Nicolle, et al. "C-terminal phosphorylation modulates ERM-1 localization and dynamics to control cortical actin organization and support lumen formation during Caenorhabditiselegans development." Development 147, no. 14 (2020): dev188011. http://dx.doi.org/10.1242/dev.188011.

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ABSTRACTERM proteins are conserved regulators of cortical membrane specialization that function as membrane-actin linkers and molecular hubs. The activity of ERM proteins requires a conformational switch from an inactive cytoplasmic form into an active membrane- and actin-bound form, which is thought to be mediated by sequential PIP2 binding and phosphorylation of a conserved C-terminal threonine residue. Here, we use the single Caenorhabditiselegans ERM ortholog, ERM-1, to study the contribution of these regulatory events to ERM activity and tissue formation in vivo. Using CRISPR/Cas9-generat

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Yonemura, Shigenobu, Motohiro Hirao, Yoshinori Doi, 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." Journal of Cell Biology 140, no. 4 (1998): 885–95. http://dx.doi.org/10.1083/jcb.140.4.885.

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Abstract. CD44 has been identified as a membrane-binding partner for ezrin/radixin/moesin (ERM) proteins, plasma membrane/actin filament cross-linkers. ERM proteins, however, are not necessarily colocalized with CD44 in tissues, but with CD43 and ICAM-2 in some types of cells. We found that glutathione-S-transferase fusion proteins with the cytoplasmic domain of CD43 and ICAM-2, as well as CD44, bound to moesin in vitro. The regions responsible for the in vitro binding of CD43 and CD44 to moesin were narrowed down to their juxta-membrane 20–30–amino acid sequences in the cytoplasmic domain. Th

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Dickson, Tracey C., C. David Mintz, Deanna L. Benson, and Stephen R. J. Salton. "Functional binding interaction identified between the axonal CAM L1 and members of the ERM family." Journal of Cell Biology 157, no. 7 (2002): 1105–12. http://dx.doi.org/10.1083/jcb.200111076.

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Ayeast two-hybrid library was screened using the cytoplasmic domain of the axonal cell adhesion molecule L1 to identify binding partners that may be involved in the regulation of L1 function. The intracellular domain of L1 bound to ezrin, a member of the ezrin, radixin, and moesin (ERM) family of membrane–cytoskeleton linking proteins, at a site overlapping that for AP2, a clathrin adaptor. Binding of bacterial fusion proteins confirmed this interaction. To determine whether ERM proteins interact with L1 in vivo, extracellular antibodies to L1 were used to force cluster the protein on cultured

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Treanor, Bebhinn, David Depoil, Andreas Bruckbauer, and Facundo D. Batista. "Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity." Journal of Experimental Medicine 208, no. 5 (2011): 1055–68. http://dx.doi.org/10.1084/jem.20101125.

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Signaling microclusters are a common feature of lymphocyte activation. However, the mechanisms controlling the size and organization of these discrete structures are poorly understood. The Ezrin-Radixin-Moesin (ERM) proteins, which link plasma membrane proteins with the actin cytoskeleton and regulate the steady-state diffusion dynamics of the B cell receptor (BCR), are transiently dephosphorylated upon antigen receptor stimulation. In this study, we show that the ERM proteins ezrin and moesin influence the organization and integrity of BCR microclusters. BCR-driven inactivation of ERM protein

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Chirivino, Dafne, Laurence Del Maestro, Etienne Formstecher, et al. "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes." Molecular Biology of the Cell 22, no. 3 (2011): 375–85. http://dx.doi.org/10.1091/mbc.e10-09-0796.

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In the degradative pathway, the progression of cargos through endosomal compartments involves a series of fusion and maturation events. The HOPS (homotypic fusion and protein sorting) complex is part of the machinery that promotes the progression from early to late endosomes and lysosomes by regulating the exchange of small GTPases. We report that an interaction between subunits of the HOPS complex and the ERM (ezrin, radixin, moesin) proteins is required for the delivery of EGF receptor (EGFR) to lysosomes. Inhibiting either ERM proteins or the HOPS complex leads to the accumulation of the EG

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Asano, Shinji. "Functional Regulation of Transport Proteins by ERM (Ezrin / Radixin / Moesin) Proteins." membrane 35, no. 6 (2010): 278–84. http://dx.doi.org/10.5360/membrane.35.278.

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27

Kobori, Takuro, Mayuka Tameishi, Chihiro Tanaka, Yoko Urashima, and Tokio Obata. "Subcellular distribution of ezrin/radixin/moesin and their roles in the cell surface localization and transport function of P-glycoprotein in human colon adenocarcinoma LS180 cells." PLOS ONE 16, no. 5 (2021): e0250889. http://dx.doi.org/10.1371/journal.pone.0250889.

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The ezrin/radixin/moesin (ERM) family proteins act as linkers between the actin cytoskeleton and P-glycoprotein (P-gp) and regulate the plasma membrane localization and functionality of the latter in various cancer cells. Notably, P-gp overexpression in the plasma membrane of cancer cells is a principal factor responsible for multidrug resistance and drug-induced mutagenesis. However, it remains unknown whether the ERM proteins contribute to the plasma membrane localization and transport function of P-gp in human colorectal cancer cells in which the subcellular localization of ERM has yet to b

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Rasmussen, Maria, R. Todd Alexander, Barbara V. Darborg, et al. "Osmotic cell shrinkage activates ezrin/radixin/moesin (ERM) proteins: activation mechanisms and physiological implications." American Journal of Physiology-Cell Physiology 294, no. 1 (2008): C197—C212. http://dx.doi.org/10.1152/ajpcell.00268.2007.

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Hyperosmotic shrinkage induces multiple cellular responses, including activation of volume-regulatory ion transport, cytoskeletal reorganization, and cell death. Here we investigated the possible roles of ezrin/radixin/moesin (ERM) proteins in these events. Osmotic shrinkage of Ehrlich Lettre ascites cells elicited the formation of long microvillus-like protrusions, rapid translocation of endogenous ERM proteins and green fluorescent protein-tagged ezrin to the cortical region including these protrusions, and Thr567/564/558 (ezrin/radixin/moesin) phosphorylation of cortical ERM proteins. Reduc

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Matsui, Takeshi, Masato Maeda, Yoshinori Doi, et al. "Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association." Journal of Cell Biology 140, no. 3 (1998): 647–57. http://dx.doi.org/10.1083/jcb.140.3.647.

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The ezrin/radixin/moesin (ERM) proteins are involved in actin filament/plasma membrane interaction that is regulated by Rho. We examined whether ERM proteins are directly phosphorylated by Rho- associated kinase (Rho-kinase), a direct target of Rho. Recombinant full-length and COOH-terminal half radixin were incubated with constitutively active catalytic domain of Rho-kinase, and ∼30 and ∼100% of these molecules, respectively, were phosphorylated mainly at the COOH-terminal threonine (T564). Next, to detect Rho-kinase–dependent phosphorylation of ERM proteins in vivo, we raised a mAb that reco

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Zegers, Ingrid, Thomas Keller, Wiebke Schreiber, et al. "Characterization of the New Serum Protein Reference Material ERM-DA470k/IFCC: Value Assignment by Immunoassay." Clinical Chemistry 56, no. 12 (2010): 1880–88. http://dx.doi.org/10.1373/clinchem.2010.148809.

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BACKGROUND The availability of a suitable matrix reference material is essential for standardization of the immunoassays used to measure serum proteins. The earlier serum protein reference material ERM-DA470 (previously called CRM470), certified in 1993, has led to a high degree of harmonization of the measurement results. A new serum protein material has now been prepared and its suitability in term of homogeneity and stability has been verified; after characterization, the material has been certified as ERM-DA470k/IFCC. METHODS We characterized the candidate reference material for 14 protein

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Winckler, B., C. Gonzalez Agosti, M. Magendantz, and F. Solomon. "Analysis of a cortical cytoskeletal structure: a role for ezrin-radixin-moesin (ERM proteins) in the marginal band of chicken erythrocytes." Journal of Cell Science 107, no. 9 (1994): 2523–34. http://dx.doi.org/10.1242/jcs.107.9.2523.

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We are studying how the cytoskeleton determines cell shape, using a simple model system, the marginal band of chicken erythrocytes. We previously identified a minor component of the marginal band by a monoclonal antibody, called 13H9 (Birgbauer and Solomon (1989). J. Cell Biol. 109, 1609–1620; Goslin et al. (1989). J. Cell Biol. 109, 1621–1631). mAb 13H9 also binds to the leading edges of fibroblasts and to neuronal growth cones and recognizes the cytoskeletal protein ezrin. In recent years, two proteins with a high degree of homology to ezrin were identified: moesin and radixin, together comp

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Baeyens, Nicolas, Sandrine Horman, Didier Vertommen, Mark Rider, and Nicole Morel. "Identification and functional implication of a Rho kinase-dependent moesin-EBP50 interaction in noradrenaline-stimulated artery." American Journal of Physiology-Cell Physiology 299, no. 6 (2010): C1530—C1540. http://dx.doi.org/10.1152/ajpcell.00175.2010.

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Ezrin, radixin, and moesin (ERM) proteins are known to be substrates of Rho kinase (ROCK), a key player in vascular smooth muscle regulation. Their function in arteries remains to be elucidated. The objective of the present study was to investigate ERM phosphorylation and function in rat aorta and mesenteric artery and the influence of ERM-binding phosphoprotein 50 (EBP50), a scaffold partner of ERM proteins in several cell types. In isolated arteries, ERM proteins are phosphorylated by PKC and ROCK with different kinetics after either agonist stimulation or KCl-induced depolarization. Immunop

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Cannon, J. L., P. D. Mody, K. M. Blaine, et al. "CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation." Molecular Biology of the Cell 22, no. 7 (2011): 954–63. http://dx.doi.org/10.1091/mbc.e10-07-0586.

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Cell polarization is a key feature of cell motility, driving cell migration to tissues. CD43 is an abundantly expressed molecule on the T-cell surface that shows distinct localization to the migrating T-cell uropod and the distal pole complex (DPC) opposite the immunological synapse via association with the ezrin-radixin-moesin (ERM) family of actin regulatory proteins. CD43 regulates multiple T-cell functions, including T-cell activation, proliferation, apoptosis, and migration. We recently demonstrated that CD43 regulates T-cell trafficking through a phosphorylation site at Ser-76 (S76) with

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Mori, T., K. Kitano, S. Terawaki, R. Maesaki, Y. Fukami, and T. Hakoshima. "Structural basis for CD44 recognition by ERM proteins." Acta Crystallographica Section A Foundations of Crystallography 64, a1 (2008): C233—C234. http://dx.doi.org/10.1107/s0108767308092490.

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35

Terawaki, Shin-ichi, Ryoko Maesaki, and Toshio Hakoshima. "Structural Basis for NHERF Recognition by ERM Proteins." Structure 14, no. 4 (2006): 777–89. http://dx.doi.org/10.1016/j.str.2006.01.015.

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36

Louvet-Vallée, Sophie. "ERM proteins: From cellular architecture to cell signaling." Biology of the Cell 92, no. 5 (2000): 305–16. http://dx.doi.org/10.1016/s0248-4900(00)01078-9.

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37

Mangeat, Paul, Christian Roy, and Marianne Martin. "ERM proteins in cell adhesion and membrane dynamics." Trends in Cell Biology 9, no. 5 (1999): 187–92. http://dx.doi.org/10.1016/s0962-8924(99)01544-5.

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Fiévet, Bruno, Daniel Louvard, and Monique Arpin. "ERM proteins in epithelial cell organization and functions." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1773, no. 5 (2007): 653–60. http://dx.doi.org/10.1016/j.bbamcr.2006.06.013.

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Mori, Tomoyuki, Ken Kitano, Shin-ichi Terawaki, Ryoko Maesaki, Yayoi Fukami, and Toshio Hakoshima. "Structural Basis for CD44 Recognition by ERM Proteins." Journal of Biological Chemistry 283, no. 43 (2008): 29602–12. http://dx.doi.org/10.1074/jbc.m803606200.

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Mintz, C. David, Ioana Carcea, Daniel G. McNickle, et al. "ERM proteins regulate growth cone responses to Sema3A." Journal of Comparative Neurology 510, no. 4 (2008): 351–66. http://dx.doi.org/10.1002/cne.21799.

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Brown, Martin J., Ruchika Nijhara, John A. Hallam, et al. "Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization." Blood 102, no. 12 (2003): 3890–99. http://dx.doi.org/10.1182/blood-2002-12-3807.

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Abstract Lymphocyte microvilli mediate initial rolling-adhesion along endothelium but are lost during transmigration from circulation to tissue. However, the mechanism for resorption of lymphocyte microvilli remains unexplored. We show that chemokine stimulation of human peripheral blood T (PBT) cells is sufficient to induce rapid resorption of microvilli. Microvilli in other cells are regulated by ezrin/radixin/moesin (ERM) proteins, which link the plasma membrane to the cortical F-actin cytoskeleton; maintenance of these linkages requires ERM activation, reflected by phosphorylation at a spe

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Hayashi, K., S. Yonemura, T. Matsui, and S. Tsukita. "Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues." Journal of Cell Science 112, no. 8 (1999): 1149–58. http://dx.doi.org/10.1242/jcs.112.8.1149.

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Ezrin/radixin/moesin (ERM) proteins are thought to play an important role in organizing cortical actin-based cytoskeletons through cross-linkage of actin filaments with integral membrane proteins. Recent in vitro biochemical studies have revealed that ERM proteins phosphorylated on their COOH-terminal threonine residue (CPERMs) are active in their cross-linking activity, but this has not yet been evaluated in vivo. To immunofluorescently visualize CPERMs in cultured cells as well as tissues using a mAb specific for CPERMs, we developed a new fixation protocol using trichloroacetic acid (TCA) a

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Hoshi, Yutaro, Yasuo Uchida, Takashi Kuroda, et al. "Distinct roles of ezrin, radixin and moesin in maintaining the plasma membrane localizations and functions of human blood–brain barrier transporters." Journal of Cerebral Blood Flow & Metabolism 40, no. 7 (2019): 1533–45. http://dx.doi.org/10.1177/0271678x19868880.

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The purpose of this study was to clarify the roles of ERM proteins (ezrin/radixin/moesin) in the regulation of membrane localization and transport activity of transporters at the human blood–brain barrier (BBB). Ezrin or moesin knockdown in a human in vitro BBB model cell line (hCMEC/D3) reduced both BCRP and GLUT1 protein expression levels on the plasma membrane. Radixin knockdown reduced not only BCRP and GLUT1, but also P-gp membrane expression. These results indicate that P-gp, BCRP and GLUT1 proteins are maintained on the plasma membrane via different ERM proteins. Furthermore, moesin kno

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Solinet, Sara, Kazi Mahmud, Shannon F. Stewman, et al. "The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex." Journal of Cell Biology 202, no. 2 (2013): 251–60. http://dx.doi.org/10.1083/jcb.201304052.

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Ezrin, Radixin, and Moesin (ERM) proteins play important roles in many cellular processes including cell division. Recent studies have highlighted the implications of their metastatic potential in cancers. ERM’s role in these processes is largely attributed to their ability to link actin filaments to the plasma membrane. In this paper, we show that the ERM protein Moesin directly binds to microtubules in vitro and stabilizes microtubules at the cell cortex in vivo. We identified two evolutionarily conserved residues in the FERM (4.1 protein and ERM) domains of ERMs that mediated the associatio

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McCartney, B. M., and R. G. Fehon. "Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin." Journal of Cell Biology 133, no. 4 (1996): 843–52. http://dx.doi.org/10.1083/jcb.133.4.843.

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Interest in members of the protein 4.1 super-family, which includes the ezrin-radixin-moesin (ERM) group, has been stimulated recently by the discovery that the human neurofibromatosis 2 (NF2) tumor suppressor gene encodes an ERM-like protein, merlin. Although many proteins in this family are thought to act by linking the actin-based cytoskeleton to transmembrane proteins, the cellular functions of merlin have not been defined. To investigate the cellular and developmental functions of these proteins, we have identified and characterized Drosophila homologues of moesin (Dmoesin) and of the NF2

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Orian-Rousseau, Véronique, Helen Morrison, Alexandra Matzke, et al. "Hepatocyte Growth Factor-induced Ras Activation Requires ERM Proteins Linked to Both CD44v6 and F-Actin." Molecular Biology of the Cell 18, no. 1 (2007): 76–83. http://dx.doi.org/10.1091/mbc.e06-08-0674.

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In several types of cells, the activation of the receptor tyrosine kinase c-Met by its ligand hepatocyte growth factor (HGF) requires the coreceptor CD44v6. The CD44 extracellular domain is necessary for c-Met autophosphorylation, whereas the intracellular domain is required for signal transduction. We have already shown that the CD44 cytoplasmic tail recruits ezrin, radixin and moesin (ERM) proteins to the complex of CD44v6, c-Met, and HGF. We have now defined the function of the ERM proteins and the step they promote in the signaling cascade. The association of ERM proteins to the coreceptor

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Iwase, Akira, Ruoqian Shen, Daniel Navarro, and David M. Nanus. "Direct Binding of Neutral Endopeptidase 24.11 to Ezrin/Radixin/Moesin (ERM) Proteins Competes with the Interaction of CD44 with ERM Proteins." Journal of Biological Chemistry 279, no. 12 (2004): 11898–905. http://dx.doi.org/10.1074/jbc.m212737200.

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Phang, Juanita M., Stephen J. Harrop, Anthony P. Duff, et al. "Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin." Biochemical Journal 473, no. 18 (2016): 2763–82. http://dx.doi.org/10.1042/bcj20160541.

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Ezrin is a member of the ERM (ezrin–radixin–moesin) family of proteins that have been conserved through metazoan evolution. These proteins have dormant and active forms, where the latter links the actin cytoskeleton to membranes. ERM proteins have three domains: an N-terminal FERM [band Four-point-one (4.1) ERM] domain comprising three subdomains (F1, F2, and F3); a helical domain; and a C-terminal actin-binding domain. In the dormant form, FERM and C-terminal domains form a stable complex. We have determined crystal structures of the active FERM domain and the dormant FERM:C-terminal domain c

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Hebert, A. M., B. DuBoff, J. B. Casaletto, A. B. Gladden, and A. I. McClatchey. "Merlin/ERM proteins establish cortical asymmetry and centrosome position." Genes & Development 26, no. 24 (2012): 2709–23. http://dx.doi.org/10.1101/gad.194027.112.

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Fehon, Richard G., Andrea I. McClatchey, and Anthony Bretscher. "Organizing the cell cortex: the role of ERM proteins." Nature Reviews Molecular Cell Biology 11, no. 4 (2010): 276–87. http://dx.doi.org/10.1038/nrm2866.

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