Direct interaction of actin filaments with <scp>F</scp>‐<scp>BAR</scp> protein pacsin2

Košťan, Július; Salzer, Ulrich; Orlova, Albina; Törö, I; Hodnik, Vesna; Senju, Yosuke; Zou, Juan; Schreiner, Claudia; Steiner, Julia; Meriläinen, Jari; Nikki, Marko; Virtanen, Ismo; Carugo, Oliviero; Rappsilber, Juri; Lappalainen, Pekka; Lehto, V.‐P.; Anderluh, Gregor; Egelman, Edward H.; Djinović-Carugo, Kristina

doi:10.15252/embr.201439267

Cited by 54 publications

(71 citation statements)

References 42 publications

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“…hBin1 and its BAR domain do not only bind to F‐actin, but also stabilize F‐actin in a depolymerization assays. This stabilization was also observed for pacsin2 at higher concentrations . In contrast to pacsin2, hBin1 binding to actin filaments could partly protect them from cofilin‐mediated disassembly.…”

Section: Discussionmentioning

confidence: 66%

“…The crosslinking was carried out as described in . Briefly, F‐actin and hBin1 (isoform 1) or dBAR were mixed at the indicated concentrations in 10 mM PIPES, 50 mM KCl, 2 mM MgCl 2 , pH 6.8 and incubated for 30 min, before adding the EDC crosslinker (1‐ethyl‐3‐(3‐dimethylaminopropyl)carbodiimide hydrochloride; Thermo Fisher Scientific) at a final concentration of 1 mM.…”

Section: Methodsmentioning

confidence: 99%

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Bin1 directly remodels actin dynamics through its BAR domain

et al. 2017

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Endocytic processes are facilitated by both curvature-generating BAR-domain proteins and the coordinated polymerization of actin filaments. Under physiological conditions, the N-BAR protein Bin1 has been shown to sense and curve membranes in a variety of cellular processes. Recent studies have identified Bin1 as a risk factor for Alzheimer's disease, although its possible pathological function in neurodegeneration is currently unknown. Here, we report that Bin1 not only shapes membranes, but is also directly involved in actin binding through its BAR domain. We observed a moderate actin bundling activity by human Bin1 and describe its ability to stabilize actin filaments against depolymerization. Moreover, Bin1 is also involved in stabilizing tau-induced actin bundles, which are neuropathological hallmarks of Alzheimer's disease. We also provide evidence for this effect , where we observed that downregulation of Bin1 in a model of tauopathy significantly reduces the appearance of tau-induced actin inclusions. Together, these findings reveal the ability of Bin1 to modify actin dynamics and provide a possible mechanistic connection between Bin1 and tau-induced pathobiological changes of the actin cytoskeleton.

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Section: Discussionmentioning

confidence: 66%

Section: Methodsmentioning

confidence: 99%

Bin1 directly remodels actin dynamics through its BAR domain

et al. 2017

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“…Furthermore, the reported interaction between PICK1 and F-actin in vitro was found to be merely caused by unspecific, probably electrostatic, interactions (Madasu et al, 2015). Electrostatic interactions with F-actin have also been observed in recent in vitro reconstitution studies using actin and the F-BAR protein syndapin II (Kostan et al, 2014). It will be interesting to clarify whether BAR domain proteins use their curved, positively charged BAR domain interfaces for direct binding of actin or actin-related molecules such as those incorporated in the Arp2/3 complex, or whether their crosstalk with actin-filament-promoting factors under physiological conditions instead requires interactions between other domains, such as the SH3-domain-mediated interactions of syndapin or CIP4/Toca subfamily members with activators of the Arp2/3 complex.…”

Section: Box 3 the Gtpase Cyclementioning

confidence: 89%

Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

Kessels

Qualmann

2015

Journal of Cell Science

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A plethora of cell biological processes involve modulations of cellular membranes. By using extended lipid-binding interfaces, some proteins have the power to shape membranes by attaching to them. Among such membrane shapers, the superfamily of Bin–Amphiphysin–Rvs (BAR) domain proteins has recently taken center stage. Extensive structural work on BAR domains has revealed a common curved fold that can serve as an extended membrane-binding interface to modulate membrane topologies and has allowed the grouping of the BAR domain superfamily into subfamilies with structurally slightly distinct BAR domain subtypes (N-BAR, BAR, F-BAR and I-BAR). Most BAR superfamily members are expressed in the mammalian nervous system. Neurons are elaborately shaped and highly compartmentalized cells. Therefore, analyses of synapse formation and of postsynaptic reorganization processes (synaptic plasticity) – a basis for learning and memory formation – has unveiled important physiological functions of BAR domain superfamily members. These recent advances, furthermore, have revealed that the functions of BAR domain proteins include different aspects. These functions are influenced by the often complex domain organization of BAR domain proteins. In this Commentary, we review these recent insights and propose to classify BAR domain protein functions into (1) membrane shaping, (2) physical integration, (3) action through signaling components, and (4) suppression of other BAR domain functions.

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“…The mechanism of how EHD2 regulates caveolae motility and its association with stress fibers remains to be identified. Pacsin2, which binds to EHD2 (Moren et al, 2012), could link caveolae to actin as it has been recently shown to directly interact with actin (Kostan et al, 2014) (Fig. 2).…”

Section: Introductionmentioning

confidence: 99%

Caveolae – mechanosensitive membrane invaginations linked to actin filaments

Echarri

Pozo

2015

Journal of Cell Science

168

213

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An essential property of the plasma membrane of mammalian cells is its plasticity, which is required for sensing and transmitting of signals, and for accommodating the tensional changes imposed by its environment or its own biomechanics. Caveolae are unique invaginated membrane nanodomains that play a major role in organizing signaling, lipid homeostasis and adaptation to membrane tension. Caveolae are frequently associated with stress fibers, a major regulator of membrane tension and cell shape. In this Commentary, we discuss recent studies that have provided new insights into the function of caveolae and have shown that trafficking and organization of caveolae are tightly regulated by stress-fiber regulators, providing a functional link between caveolae and stress fibers. Furthermore, the tension in the plasma membrane determines the curvature of caveolae because they flatten at high tension and invaginate at low tension, thus providing a tension-buffering system. Caveolae also regulate multiple cellular pathways, including RhoA-driven actomyosin contractility and other mechanosensitive pathways, suggesting that caveolae could couple mechanotransduction pathways to actin-controlled changes in tension through their association with stress fibers. Therefore, we argue here that the association of caveolae with stress fibers could provide an important strategy for cells to deal with mechanical stress.

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Direct interaction of actin filaments with F‐BAR protein pacsin2

Cited by 54 publications

References 42 publications

Bin1 directly remodels actin dynamics through its BAR domain

Bin1 directly remodels actin dynamics through its BAR domain

Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

Caveolae – mechanosensitive membrane invaginations linked to actin filaments

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