Phosphatidylinositol 4,5-Bisphosphate Alters the Number of Attachment Sites between Ezrin and Actin Filaments

Braunger, Julia A.; Brückner, Bastian Rouven; Nehls, Stefan; Pietuch, Anna; Gerke, Volker; Mey, Ingo; Janshoff, Andreas; Steinem, Claudia

doi:10.1074/jbc.m113.530659

Cited by 45 publications

(63 citation statements)

References 57 publications

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“…This regulation could be by direct binding or by indirect mechanisms involving interacting proteins whose function depends on PIP2 binding. A good example of that is the Erzin-PIP2 interaction that strengthens actin binding to the cellular membrane and modulates cell adhesion and morphology [97]. Similarly, it has been proposed that the membrane protein Pirt can modulate TRPV1 activity trough a PIP2-dependent mechanism [52].…”

Section: Modulation Of Trp Channel Function By Phosphoinositidesmentioning

confidence: 99%

TRP channels interaction with lipids and its implications in disease

Taberner

Fernández‐Ballester

Fernández-Carvajal

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Transient receptor potential (TRP) proteins are a family of ion channels central for sensory signaling. These receptors and, in particular, those involved in thermal sensing are also involved in pain signaling. Noteworthy, thermosensory receptors are polymodal ion channels that respond to both physical and chemical stimuli, thus integrating different environmental clues. In addition, their activity is modulated by algesic agents and lipidergic substances that are primarily released in pathological states. Lipids and lipid-like molecules have been found that can directly activate some thermosensory channels or modulate their activity by either potentiating or inhibiting it. To date, more than 50 endogenous lipids that can regulate TRP channel activity in sensory neurons have been described, thus representing the majority of known endogenous TRP channel modulators. Lipid modulators of TRP channels comprise lipids from a variety of metabolic pathways, including metabolites of the cyclooxygenase, lipoxygenase and cytochrome-P450 pathways, phospholipids and lysophospholipids. Therefore, TRP-channels are able to integrate and interpret incoming signals from the different metabolic lipid pathways. Taken together, the large number of lipids that can activate, sensitize or inhibit neuronal TRP-channels highlights the pivotal role of these molecules in sensory biology as well as in pain transduction and perception. This article is part of a Special Issue entitled: Lipid-protein interactions. Guest Editors: Amitabha Chattopadhyay and Jean-Marie Ruysschaert.

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Section: Modulation Of Trp Channel Function By Phosphoinositidesmentioning

confidence: 99%

TRP channels interaction with lipids and its implications in disease

Taberner

Fernández‐Ballester

Fernández-Carvajal

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…[19]); (ii) membrane interaction with cytoskeletal components such as sub-membrane acto-myosin cortex [17] and acto-myosin network driving cell motion along external substrates [20,21]; and (iii) forces resulting from cell adhesion to and spreading on external substrates [2] and forces caused by cell-cell adhesion [22]. In specific instances, tension is often produced by interplay between these primary factors.…”

Section: Membrane Tensionmentioning

confidence: 99%

Membrane tension and membrane fusion

Kozlov

Chernomordik

2015

Current Opinion in Structural Biology

141

135

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Diverse cell biological processes that involve shaping and remodeling of cell membranes are regulated by membrane lateral tension. Here we focus on the role of tension in driving membrane fusion. We discuss the physics of membrane tension, forces that can generate the tension in plasma membrane of a cell, and the hypothesis that tension powers expansion of membrane fusion pores in late stages of cell-to-cell and exocytotic fusion. We propose that fusion pore expansion can require unusually large membrane tensions or, alternatively, low line tensions of the pore resulting from accumulation in the pore rim of membrane-bending proteins. Increase of the intermembrane distance facilitates the reaction. Graphic abstractFusion pore expansion in the contact zone between two membranes docked together by the adhesion proteins increases the perimeter of the energy-intensive pore edge and has to be driven by membrane tension. Accumulation of the membrane-bending proteins at the pore rim lowers the pore edge energy (line tension of the pore) and, thus, lowers the membrane tension required for the pore expansion.

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“…This complexity can be reduced by employing biomimetic systems comprising only a limited number of components. Such systems have been introduced into the field of ERM proteins in an attempt to understand their molecular behavior in complex systems (17)(18)(19)(20)(21). In addition, in vitro experiments using well-defined lipid membranes and purified proteins can provide quantitative information about protein-membrane interactions and conformational changes associated with the activation process of ezrin.…”

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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Phosphatidylinositol 4,5-Bisphosphate Alters the Number of Attachment Sites between Ezrin and Actin Filaments

Cited by 45 publications

References 57 publications

TRP channels interaction with lipids and its implications in disease

TRP channels interaction with lipids and its implications in disease

Membrane tension and membrane fusion

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

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