The ezrin protein family: membrane-cytoskeleton interactions and disease associations

Vaheri, Antti; Carpén, Olli; Heiska, Leena; Helander, Tuula; Jääskeläinen, Juha E.; Majander-Nordenswan, Päivi; Sainio, Markku; Timonen, Tuomo; Turunen, Ossi

doi:10.1016/s0955-0674(97)80119-6

Cited by 187 publications

(131 citation statements)

References 58 publications

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“…They vary greatly in size, with some reaching enormous lengths of up to 0.5 mm and ranking second only to the special processes of neuronal cells, i.e., neurites. Their cytoskeletal core is essentially based on a system of actin microfilament bundles, fortified and attached to the cell membrane via myosin, α-actinin, ezrin, and probably other morphogenic actin-binding proteins that have yet to be identified (for candidates see, e.g., Bonilha et al 1999;Vaheri et al 1997;Bretscher et al 2002;Kobielak et al 2004) and of microtubules (cf. Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Although this protein originally and typically has been reported in microvilli and other organized protrusions of epithelial cells, it has subsequently also been identified in cell extensions of diverse types of mesenchymal cells (for reviews, see Vaheri et al 1997;Bretscher et al 2002). Moreover, whereas its roles as a potentially actin-binding and actin microfilamentto-membrane linking protein and as an adhering junctionassociated protein have been demonstrated in many examples, it has more recently also been reported to act as a signaling and life-protecting protein (e.g., Gautreau et al 1999;Bretscher et al 2002; and references cited therein) and may be more generally involved in morphogenic processes, probably tightly controlled by kinase activities (Bonilha et al 1999;Lan et al 2006).…”

Section: Discussionmentioning

confidence: 99%

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Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

et al. 2007

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Substrate-adherent cultured cells derived from human bone marrow or umbilical cord blood ("mesenchymal stem cells") are of special interest for regenerative medicine. We report that such cells, which can display considerable heterogeneity with respect to their cytoskeletal protein complement, are often interconnected by special tentacle-like cell processes contacting one or several other cells. These processus adhaerentes, studded with many (usually small) puncta adhaerentia and varying greatly in length (up to more than 400 μm long), either contact each other in the intercellular space ("ET touches") or insert in a tight-fitting manner into deep plasma membrane invaginations (recessus adhaerentes), thus forming a novel kind of long (up to 50 μm) continuous cuff-like junction (manubria adhaerentia). The cell processes contain an actin microfilament core that is stabilized with ezrin, α-actinin, and myosin and accompanied by microtubules, and their adhering junctions are characterized by a molecular complement comprising the transmembrane glycoproteins N-cadherin and cadherin-11, in combination with the cytoplasmic plaque proteins α-and β-catenin, together with p120 ctn , plakoglobin, and afadin. The processes are also highly dynamic and rapidly foreshorten as cell colonies approach a denser state of cell packing. These structures are obviously able to establish cell-cell connections, even over long distances, and can form deep-rooted and tight cell-cell adhesions. The possible relationship to similar cell processes in the embryonic primary mesenchyme and their potential in cell sorting and tissue formation processes in the body are discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

et al. 2007

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“…Immunoblotting analysis and immunofluorescence microscopy revealed that in most cultured cells all ERM proteins are coexpressed and co-localized but that in organs their expression and distribution pattern appear to be regulated in a cell type-specific manner (1)(2)(3)(4)(5)(6)(7). Immunofluorescence studies of cultured fibroblasts and epithelial cells have revealed that ERM proteins are co-expressed and co-concentrated at cell-surface structures such as microvilli, filopodia, uropods, ruffling membranes, retraction fibers, and cell adhesion sites where actin filaments are associated with plasma membranes (8, 14 -17) (Fig.…”

Section: Subcellular Distribution and Functions Of Erm Proteinsmentioning

confidence: 99%

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

Tsukita¹,

Yonemura²

1999

Journal of Biological Chemistry

438

377

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“…H19 -7/IGF-IR cells were seeded at 2 ϫ 10 5 in a 6-well plate coated with poly-L-lysine. For glutamate treatment, the cells were cultured in serum-free DMEM for 18 h and then stimulated with or without 100 M glutamate for various periods (2,5,10,30, and 60 min). fetal bovine serum.…”

Section: Treatment Of Animals and The Preparation Of Hippocampal Lysamentioning

confidence: 99%

RhoA and Rho Kinase-dependent Phosphorylation of Moesin at Thr-558 in Hippocampal Neuronal Cells by Glutamate

Jeon¹,

Kim²,

Park³

et al. 2002

Journal of Biological Chemistry

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When we were studying phosphorylated proteins in the rat brain after electroconvulsive shock (ECS), we observed the rapid phosphorylation of a 75-kDa protein, which cross-reacted with the anti-phospho-p70 S6 kinase antibody. The phosphorylated protein was purified and identified as moesin, a member of the ezrin/radixin/ moesin (ERM) family and a general cross-linker between cortical actin filaments and plasma membranes. The purified moesin from rat brain was phosphorylated at serine and threonine residues. Moesin was rapidly phosphorylated at the threonine 558 residue after ECS in the rat hippocampus, peaked at 1 min, and returned to the basal level by 2 min after ECS. To investigate the mechanism of moesin phosphorylation in neuronal cells, we stimulated a rat hippocampal progenitor cell, H19 -7/ IGF-IR, with glutamate, and observed the increased phosphorylation of moesin at Thr-558. Glutamate transiently activated RhoA, and constitutively active RhoA increased the basal level phosphorylation of moesin. The inhibition of RhoA and its effector, Rho kinase, abolished increased Thr-558 phosphorylation by glutamate in H19 -7/IGF-IR cells, suggesting that the phosphorylation of moesin at Thr-558 in H19 -7/IGF-IR cells by glutamate is mediated by RhoA and Rho kinase activation. Electroconvulsive shock (ECS)1 has been used for the treatments of psychiatric disorders such as depression, schizophrenia, and manic-depressive illness. Although the mechanism of the treatment has not been elucidated, recent progress in the cellular and molecular biology of neuronal tissues has enabled neuronal functions to be linked to the regulation of gene expression and intracellular signal transduction (1). Previously, we reported (4) that ECS induces the expressions of various immediate early genes such as c-fos, junB, and TiS-8 and that it suppresses the expression of inositol 1,4,5-triphosphate kinase and inositol 1,4,5-triphosphate receptor genes. We also observed (2-5, 7) that ECS caused the phosphorylation of many signaling molecules, including those in the Pyk2-Ras-Raf-MEK-ERK pathway, and of stress-signaling pathways in various rat brain regions.Earlier we reported that ECS induces the phosphorylation of CREB in the rat hippocampus (6). Several protein kinases have been suggested to be CREB kinases in neuronal tissues, and we looked for protein kinases potentially responsible for CREB phosphorylation. When we were studying the phosphorylation of one of the suggested CREB kinases, ribosomal S6 kinase (S6K), we observed that a 75-kDa protein in the rat hippocampus was rapidly phosphorylated after ECS. This was detected by an antibody specific to phospho-p70 S6K. The protein was not detected by the anti-p70 S6K antibody, suggesting that this protein was detected nonspecifically by an anti-phospho-p70-S6K antibody. So we purified and identified this protein as moesin (membrane-organizing extension spike protein), a member of the ezrin/radixin/moesin (ERM) family of proteins.

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The ezrin protein family: membrane-cytoskeleton interactions and disease associations

Cited by 187 publications

References 58 publications

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

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

RhoA and Rho Kinase-dependent Phosphorylation of Moesin at Thr-558 in Hippocampal Neuronal Cells by Glutamate

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