The Role of BAR Domain Proteins in the Regulation of Membrane Dynamics

Derkacheva, N. I.; Polevova, Svetlana; Sokolova, Olga

doi:10.32607/20758251-2016-8-4-60-69

Cited by 34 publications

(31 citation statements)

References 103 publications

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“…The BAR domain is found in many proteins implicated in various cellular processes, most of which are related to membrane remodeling (Stanishneva-Konovalova et al, 2016;Carman and Dominguez, 2018;Nishimura et al, 2018;Simunovic et al, 2019). BAR domains typically form banana-shaped homodimers, where each protomer consists of three-helix antiparallel coiledcoil structure.…”

Section: Bar Domain-containing Proteinsmentioning

confidence: 99%

“…Most BAR domain proteins also contain auxiliary domains involved in the interactions with other proteins or with membranes (Mim et al, 2012;Carman and Dominguez, 2018). Based on their structural properties, BAR domain proteins can be classified into three main groups: a classical BAR (including N-BAR), F-BAR, and I-BAR (Ahmed et al, 2010;Stanishneva-Konovalova et al, 2016;Nishimura et al, 2018). Proteins belonging to the N-BAR subgroup contain an N-terminal sequence H0 that folds into an AH upon membrane binding.…”

Section: Bar Domain-containing Proteinsmentioning

confidence: 99%

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Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission

Zhukovsky

Filograna

Luini

et al. 2019

Front. Cell Dev. Biol.

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Renard et al. (2018) suggested to classify membrane fission mechanisms into two main categories: active fission (with the direct consumption of cellular energy by nucleoside triphosphate hydrolysis) and passive fission (without the direct use of energy). Many membrane fission processes are dependent on the interaction of fission-inducing proteins with specific lipid molecules (see below). In some cases, passive fission might be energized indirectly, via the energy used in the synthesis of these lipid cofactors (Gopaldass et al., 2017). Moreover, membrane fission processes can be classified into two types: "normal topology fission" (membrane-enclosed compartments bud toward the cytosol) and "reverse topology fission" (membrane-enclosed compartments bud away from the cytosol) (

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Section: Bar Domain-containing Proteinsmentioning

confidence: 99%

Section: Bar Domain-containing Proteinsmentioning

confidence: 99%

Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission

Zhukovsky

Filograna

Luini

et al. 2019

Front. Cell Dev. Biol.

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“…With respect to putative functionality, Tyrosine 792 is located in the proline/serine rich domain between the GAP and SH3 domains and thus is poised to effect SH3-mediated protein-protein interactions and intracellular localization [39]. However, it is formally possible that this phospho-site could promote GRAF3 activity since SH3 domain-mediated interactions have been shown to autoinhibit the membrane-binding capabilities of N-Bar and F-Bar domains in the related proteins endophillin and syndapin, respectively [65][66][67]. While our data reveals that this Y792 is not a major target for Src or FAK, it will be of future interest to determine if and how this or other post-translational modifications impact GRAF3 activity.…”

Section: Discussionmentioning

confidence: 99%

Molecular Regulation of the RhoGAP GRAF3 and Its Capacity to Limit Blood Pressure In Vivo

Dee

Xue

Mack

et al. 2020

Cells

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Anti-hypertensive therapies are usually prescribed empirically and are often ineffective. Given the prevalence and deleterious outcomes of hypertension (HTN), improved strategies are needed. We reported that the Rho-GAP GRAF3 is selectively expressed in smooth muscle cells (SMC) and controls blood pressure (BP) by limiting the RhoA-dependent contractility of resistance arterioles. Importantly, genetic variants at the GRAF3 locus controls BP in patients. The goal of this study was to validate GRAF3 as a druggable candidate for future anti-HTN therapies. Importantly, using a novel mouse model, we found that modest induction of GRAF3 in SMC significantly decreased basal and vasoconstrictor-induced BP. Moreover, we found that GRAF3 protein toggles between inactive and active states by processes controlled by the mechano-sensing kinase, focal adhesion kinase (FAK). Using resonance energy transfer methods, we showed that agonist-induced FAK-dependent phosphorylation at Y376GRAF3 reverses an auto-inhibitory interaction between the GAP and BAR-PH domains. Y376 is located in a linker between the PH and GAP domains and is invariant in GRAF3 homologues and a phosphomimetic E376GRAF3 variant exhibited elevated GAP activity. Collectively, these data provide strong support for the future identification of allosteric activators of GRAF3 for targeted anti-hypertensive therapies.

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“…However, there is an energetic cost to forming non-spherical lipid bilayers, and an array of lipid, protein, and cytoskeletal components are required [121]. For example, BAR (Bin/amphiphysin/Rvs) proteins electrostatically bind to membranes and oligomerise to induce concave or convex curvature [123,124]. Similarly, the dynamin, ESCRT (endosomal sorting complexes required for transport) and clathrin proteins are involved in directing membrane curvature in vesicle formation and endocyotosis [10,89,125].…”

Section: Bio-inspired Membrane Shapingmentioning

confidence: 99%

The Fusion of Lipid and DNA Nanotechnology

Darley

Singh

Surace

et al. 2019

Genes

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Lipid membranes form the boundary of many biological compartments, including organelles and cells. Consisting of two leaflets of amphipathic molecules, the bilayer membrane forms an impermeable barrier to ions and small molecules. Controlled transport of molecules across lipid membranes is a fundamental biological process that is facilitated by a diverse range of membrane proteins, including ion-channels and pores. However, biological membranes and their associated proteins are challenging to experimentally characterize. These challenges have motivated recent advances in nanotechnology towards building and manipulating synthetic lipid systems. Liposomes—aqueous droplets enclosed by a bilayer membrane—can be synthesised in vitro and used as a synthetic model for the cell membrane. In DNA nanotechnology, DNA is used as programmable building material for self-assembling biocompatible nanostructures. DNA nanostructures can be functionalised with hydrophobic chemical modifications, which bind to or bridge lipid membranes. Here, we review approaches that combine techniques from lipid and DNA nanotechnology to engineer the topography, permeability, and surface interactions of membranes, and to direct the fusion and formation of liposomes. These approaches have been used to study the properties of membrane proteins, to build biosensors, and as a pathway towards assembling synthetic multicellular systems.

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The Role of BAR Domain Proteins in the Regulation of Membrane Dynamics

Cited by 34 publications

References 103 publications

Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission

Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission

Molecular Regulation of the RhoGAP GRAF3 and Its Capacity to Limit Blood Pressure In Vivo

The Fusion of Lipid and DNA Nanotechnology

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