Dynamics of ezrin and EBP50 in regulating microvilli on the apical aspect of epithelial cells

Viswanatha, Raghuvir; Bretscher, Anthony; Garbett, Damien

doi:10.1042/bst20130263

Cited by 48 publications

(66 citation statements)

References 64 publications

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“…GST-C-ERMAD bound to glutathione agarose beads was labelled with LOK kinase in the presence of [γ- 32 P]ATP, and eluted with glutathione according to protocols of Viswanatha et al (2014).…”

Section: Methodsmentioning

confidence: 99%

Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1)

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Williams

Eto

et al. 2017

eLife

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The small phosphoprotein pCPI-17 inhibits myosin light-chain phosphatase (MLCP).Current models postulate that during muscle relaxation, phosphatases other than MLCP dephosphorylate and inactivate pCPI-17 to restore MLCP activity. We show here that such hypotheses are insufficient to account for the observed rapidity of pCPI-17 inactivation in mammalian smooth muscles. Instead, MLCP itself is the critical enzyme for pCPI-17 dephosphorylation. We call the mutual sequestration mechanism through which pCPI-17 and MLCP interact inhibition by unfair competition: MLCP protects pCPI-17 from other phosphatases, while pCPI-17 blocks other substrates from MLCP's active site. MLCP dephosphorylates pCPI-17 at a slow rate that is, nonetheless, both sufficient and necessary to explain the speed of pCPI-17 dephosphorylation and the consequent MLCP activation during muscle relaxation.

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Section: Methodsmentioning

confidence: 99%

Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1)

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Williams

Eto

et al. 2017

eLife

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“…The cellular polarity is also evident by the localization of the scaffold protein phospho-ezrin ( p-Ezrin) to the apical microvilli ( Fig. 3D,D′) (Bonilha et al, 1999;Viswanatha et al, 2014). By contrast, in the Dicer1 loxP/loxP ;Dct-Cre mice the RPE cells were depigmented and smaller than normal, which resulted in a twofold increase in cell density ( Fig.…”

Section: Conditional Ablation Of Dicer1 From Rpe Cells As a Global Inmentioning

confidence: 98%

MicroRNAs of the RPE are essential for RPE differentiation and photoreceptor maturation

et al. 2015

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Dysfunction of the retinal pigmented epithelium (RPE) results in degeneration of photoreceptors and vision loss and is correlated with common blinding disorders in humans. Although many proteincoding genes are known to be expressed in RPE and are important for its development and maintenance, virtually nothing is known about the in vivo roles of non-coding transcripts. The expression patterns of microRNAs (miRNAs) have been analyzed in a variety of ocular tissues, and a few were implicated to play role in RPE based on studies in cell lines. Here, through RPE-specific conditional mutagenesis of Dicer1 or Dgcr8 in mice, the importance of miRNAs for RPE differentiation was uncovered. miRNAs were found to be dispensable for maintaining RPE fate and survival, and yet they are essential for the acquisition of important RPE properties such as the expression of genes involved in the visual cycle pathway, pigmentation and cell adhesion. Importantly, miRNAs of the RPE are required for maturation of adjacent photoreceptors, specifically for the morphogenesis of the outer segments. The alterations in the miRNA and mRNA profiles in the Dicer1-deficient RPE point to a key role of miR-204 in regulation of the RPE differentiation program in vivo and uncover the importance of additional novel RPE miRNAs. This study reveals the combined regulatory activity of miRNAs that is required for RPE differentiation and for the development of the adjacent neuroretina.

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“…ERM proteins share a common structure composed of three distinct domains: 1) the N-terminal membrane-binding domain, which has similarities to a domain in protein 4.1 and is termed the FERM domain (1); 2) the central a-helical domain; and 3) the C-terminal actin-binding domain. One member of this family, ezrin, is particularly enriched in intestinal microvilli and in filopodia (5,6). Like all ERM proteins, it can exist in at least two different states, closed (inactive) or open (active) (7).…”

Section: Introductionmentioning

confidence: 99%

Mode of Ezrin-Membrane Interaction as a Function of PIP 2 Binding and Pseudophosphorylation

Shabardina

Kramer

Gerdes

et al. 2016

Biophysical Journal

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Ezrin, a protein of the ezrin, radixin, moesin (ERM) family, provides a regulated linkage between the plasma membrane and the cytoskeleton. The hallmark of this linkage is the activation of ezrin by phosphatidylinositol-4,5-bisphosphate (PIP2) binding and a threonine phosphorylation at position 567. To analyze the influence of these activating factors on the organization of ezrin on lipid membranes and the proposed concomitant oligomer-monomer transition, we made use of supported lipid bilayers in conjunction with atomic force microscopy and fluorescence microscopy. Bilayers doped with either PIP2 as the natural receptor lipid of ezrin or a Ni-nitrilotriacetic acid-equipped lipid to bind the proteins via their His6-tags to the lipid membrane were used to bind two different ezrin variants: ezrin wild-type and ezrin T567D mimicking the phosphorylated state. Using a combination of reflectometric interference spectroscopy, atomic force microscopy, and Förster resonance energy transfer experiments, we show that only the ezrin T567D mutant, upon binding to PIP2-containing bilayers, undergoes a remarkable conformational change, which we attribute to an opening of the conformation resulting in monomeric protein on the lipid bilayer.

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Dynamics of ezrin and EBP50 in regulating microvilli on the apical aspect of epithelial cells

Cited by 48 publications

References 64 publications

Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1)

Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1)

MicroRNAs of the RPE are essential for RPE differentiation and photoreceptor maturation

Mode of Ezrin-Membrane Interaction as a Function of PIP 2 Binding and Pseudophosphorylation

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