Cortical Actin Organization: Lessons from ERM (Ezrin/Radixin/Moesin) Proteins

Tsukita, Sachiko; Yonemura, Shigenobu

doi:10.1074/jbc.274.49.34507

Cited by 440 publications

(399 citation statements)

References 72 publications

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“…Moreover, Rho-PI4P5K-PIP 2 pathway is responsible for continuous activation of ERM proteins. PI4P5K synthesizes PIP 2 and accumulates it on the membrane, and binding of PIP 2 to ERM proteins is a prerequisite for their phosphorylation and activation (Mangeat et al, 1999;Tsukita and Yonemura, 1999).…”

Section: Rhoa-pi4p5k-pip 2 Pathway Mediates Cd146-induced Erm Activationmentioning

confidence: 99%

“…Among these adaptor proteins mediating such associations, the highly conserved ezrin-radixin-moesin (ERM) proteins are crucial components that provide a regulatable link between membrane-associated proteins and the cortical cytoskeleton, and also participate in signal transductions (Bretscher et al, 2002;McClatchey, 2003). ERM proteins bind to the plasma membrane receptors at their NH 2 -terminal (NT) domains and to F-actin at their COOH-terminal (CT) domains (Bretscher et al, 1997;Tsukita and Yonemura, 1999). By inhibitory self-association through intra-or intermolecular head-to-tail interactions between the NT and CT domains, several active binding sites on ERM proteins are masked.…”

Section: Introductionmentioning

confidence: 99%

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Recognition of CD146 as an ERM-binding protein offers novel mechanisms for melanoma cell migration

et al. 2011

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Tumor cell migration is a well-orchestrated multistep process that drives cancer development and metastasis. Previous data indicated that CD146 expression correlates with malignant progression and metastatic potential of human melanoma cells. However, the exact molecular mechanism of how CD146 promotes melanoma cell migration still remains poorly understood. Here, we report that CD146 physically interacts with actin-linking ezrin-radixin-moesin (ERM) proteins and recruits ERM proteins to cell protrusions, promoting the formation and elongation of microvilli. Moreover, CD146-promoted melanoma cell migration is linked to RhoA activation and ERM phosphorylation. CD146 recruits Rho guanine nucleotide dissociation inhibitory factors 1 (RhoGDI1) through ERM proteins and thus sequesters RhoGDI1 from RhoA, which leads to upregulated RhoA activity and increased melanoma cell motility. CD146-activated RhoA also promotes further ERM phosphorylation and activation through Rho-phosphatidylinositol-4-phosphate-5-kinase-phosphatidylinositol 4,5-biphosphate pathway, which reinforces CD146/ERM association. Thus, our results provide a mechanistic basis to understand the role of CD146 in regulating human melanoma cell motility.

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Section: Rhoa-pi4p5k-pip 2 Pathway Mediates Cd146-induced Erm Activationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Recognition of CD146 as an ERM-binding protein offers novel mechanisms for melanoma cell migration

et al. 2011

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“…Ezrin, radixin and moesin belong to a family of proteins (ERM) involved in the linking of transmembrane proteins to the actin cytoskeleton. [30][31][32][33][34][35] ERM proteins expose their binding sites to both actin and membrane proteins exclusively when they are in an opened/activated form through phosphorylation. [35][36] Notably, a rapid ezrin Tyr-phosphorylation does occur following CD4 crosslinking in human T -lymphocytes.…”

mentioning

confidence: 99%

CD95/phosphorylated ezrin association underlies HIV-1 GP120/IL-2-induced susceptibility to CD95(APO-1/Fas)-mediated apoptosis of human resting CD4+T lymphocytes

et al. 2004

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CD95(APO-1/Fas)-mediated apoptosis of bystander uninfected T cells exerts a major role in the HIV-1-mediated CD4 þ T-cell depletion. HIV-1 gp120 has a key role in the induction of sensitivity of human lymphocytes to CD95-mediated apoptosis through its interaction with the CD4 receptor. Recently, we have shown the importance of CD95/ezrin/actin association in CD95-mediated apoptosis. In this study, we explored the hypothesis that the gp120-mediated CD4 engagement could be involved in the induction of susceptibility of primary human T lymphocytes to CD95-mediated apoptosis through ezrin phosphorylation and ezrin-to-CD95 association. Here, we show that gp120/IL-2 combined stimuli, as well as the direct CD4 triggering, on human primary CD4 þ T lymphocytes induced an early and stable ezrin activation through phosphorylation, consistent with the induction of ezrin/CD95 association and susceptibility to CD95-mediated apoptosis. Our results provide a new mechanism through which HIV-1-gp120 may predispose resting CD4 þ T cell to bystander CD95-mediated apoptosis and support the key role of ezrin/CD95 linkage in regulating susceptibility to CD95-mediated apoptosis.

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“…ERM proteins contain an N-terminal FERM (4.1-ezrinradixin-moesin) domain that binds to phosphatidylinositol-(4,5)phosphate and cellular membrane proteins (37). Similarly to PKC, ERM proteins become phosphorylated at their conserved C-terminal threonines upon ligand binding, thereby undergoing conformational alterations.…”

mentioning

confidence: 99%

“…To further substantiate this hypothesis, we measured the activity of Rdx, as evidenced by its threonine 564 phosphorylation (35), in time course experiments using a phosphorylation-specific antibody (37). As shown in Fig.…”

mentioning

confidence: 99%

Ezrin-Radixin-Moesin Family Proteins Are Involved in Parvovirus Replication and Spreading

Nüesch

Bär

Lachmann

et al. 2009

J Virol

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The propagation of autonomous parvoviruses is strongly dependent on the phosphorylation of the major nonstructural protein NS1 by members of the protein kinase C (PKC) family. Minute virus of mice (MVM) replication is accompanied by changes in the overall phosphorylation pattern of NS1, which is newly modified at consensus PKC sites. These changes result, at least in part, from the ability of MVM to modulate the PDK-1/PKC pathway, leading to activation and redistribution of both PDK-1 and PKC . We show that proteins of the ezrin-radixin-moesin (ERM) family are essential for virus propagation and spreading through their functions as adaptors for PKC . MVM infection led to redistribution of radixin and moesin in the cell, resulting in increased colocalization of these proteins with PKC . Radixin was found to control the PKCdriven phosphorylation of NS1 and newly synthesized capsids in vivo. Conversely, radixin phosphorylation and activation were driven by the NS1/CKII␣ complex. Altogether, these data argue for ERM proteins being both targets and modulators of parvovirus infection.

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Cortical Actin Organization: Lessons from ERM (Ezrin/Radixin/Moesin) Proteins

Cited by 440 publications

References 72 publications

Recognition of CD146 as an ERM-binding protein offers novel mechanisms for melanoma cell migration

Recognition of CD146 as an ERM-binding protein offers novel mechanisms for melanoma cell migration

CD95/phosphorylated ezrin association underlies HIV-1 GP120/IL-2-induced susceptibility to CD95(APO-1/Fas)-mediated apoptosis of human resting CD4+T lymphocytes

Ezrin-Radixin-Moesin Family Proteins Are Involved in Parvovirus Replication and Spreading

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