Conformational dynamics of actin: Effectors and implications for biological function

Hild, Gábor; Bugyi, Beáta; Nyitrai, Miklós

doi:10.1002/cm.20473

Cited by 44 publications

(45 citation statements)

References 275 publications

(401 reference statements)

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“…It is known that actin filaments acquire conformational changes in response to changes in nucleotide binding or cellular stressors (134–136). The interaction between actin filaments and various actin-binding proteins are critical for the functional differentiation of actin filaments in vivo (134;135;137). Cell polarity is dynamic and dependent on various physiological processes such as cell division, migration, and morphogenesis.…”

Section: Mitochondrial Dysfunction Modulates Cellular Morphologmentioning

confidence: 99%

Mitochondrial dysfunction and mitochondrial dynamics-The cancer connection

Srinivasan

Guha

Kashina

et al. 2017

Biochimica et Biophysica Acta (BBA) - Bioenergetics

332

230

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Mitochondrial dysfunction is a hallmark of many diseases. The retrograde signaling initiated by dysfunctional mitochondria can bring about global changes in gene expression that alters cell morphology and function. Typically, this is attributed to disruption of important mitochondrial functions, such as ATP production, integration of metabolism, calcium homeostasis and regulation of apoptosis. Recent studies showed that in addition to these factors, mitochondrial dynamics might play an important role in stress signaling. Normal mitochondria are highly dynamic organelles whose size, shape and network are controlled by cell physiology. Defective mitochondrial dynamics play important roles in human diseases. Mitochondrial DNA defects and defective mitochondrial function have been reported in many cancers. Recent studies show that increased mitochondrial fission is a pro-tumorigenic phenotype. In this paper, we have explored the current understanding of the role of mitochondrial dynamics in pathologies. We present new data on mitochondrial dynamics and dysfunction to illustrate a causal link between mitochondrial DNA defects, excessive fission, mitochondrial retrograde signaling and cancer progression.

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Section: Mitochondrial Dysfunction Modulates Cellular Morphologmentioning

confidence: 99%

Mitochondrial dysfunction and mitochondrial dynamics-The cancer connection

Srinivasan

Guha

Kashina

et al. 2017

Biochimica et Biophysica Acta (BBA) - Bioenergetics

332

230

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“…Actin is an essential protein and its regulated transition between the G-actin (soluble monomer) and F-actin (component of insoluble polymer microfilaments) states is involved in many biological processes, such as cell division, motility, and signaling. Various actin-binding proteins (ABPs) and small molecules control this transition and actin dynamics, highlighting the importance and complexity of actin organization (Hild et al, 2010). In support of the role of Mical in actin cytoskeleton organization, human Mical homologs were found to regulate actin stress fibers, although the molecular mechanisms remain to be elucidated (Giridharan et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation

Lee¹,

Péterfi²,

Hoffmann³

et al. 2013

Molecular Cell

218

223

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Summary Redox control of protein function involves oxidation and reduction of amino acid residues, but mechanisms and regulators involved are insufficiently understood. Here, we report that methionine-R-sulfoxide reductase B1 (MsrB1) regulates, in conjunction with Mical proteins, mammalian actin assembly via stereoselective methionine oxidation and reduction in a reversible, site-specific manner. Two methionine residues in actin are specifically converted to methionine-R-sulfoxide by Mical1 and Mical2 and reduced back to methionine by selenoprotein MsrB1, supporting actin disassembly and assembly, respectively. Macrophages utilize this redox control during cellular activation by stimulating MsrB1 expression and activity as a part of innate immunity. We identified the regulatory role of MsrB1 as a Mical antagonist in orchestrating actin dynamics and macrophage function. More generally, our study shows that proteins can be regulated by reversible site-specific methionine-R-sulfoxidation.

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“…Many ABPs exhibit binding preference for specific actin filament conformations in vitro . 66 ABPs might stabilize specific actin filament conformations with long-range effects, or selectively bind to preferred actin filament populations. ADF/cofilin has been shown to interact with and stabilize a specific conformational state of ADP–F-actin, and to modify the mechanical properties of the bound filaments.…”

Section: Cooperativity Of Abp-binding and F-actin Remodelingmentioning

confidence: 99%

“…It is proposed that the properties of F-actin are modified upon binding with ABP, with long-range effects that subsequently affect the binding of other ABPs. 72 Allosteric interactions can have long-range effects on individual actin filaments, maintaining the filaments in a specific conformation over biologically relevant distances, 66,70 although not necessarily over the entire length of the actin filaments. 61 Thus, binding a single ABP may be sufficient to modify the structure of the filament, explaining why additional ABPs would bind cooperatively to such filaments to form regions saturated with this ABP e.g.…”

Section: Cooperativity Of Abp-binding and F-actin Remodelingmentioning

confidence: 99%

Correlative nanoscale imaging of actin filaments and their complexes

et al. 2013

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Actin remodeling is an area of interest in biology in which correlative microscopy can bring a new way to analyze protein complexes at the nanoscale. Advances in EM, X-ray diffraction, fluorescence, and single molecule techniques have provided a wealth of information about the modulation of the F-actin structure and its regulation by actin binding proteins (ABPs). Yet, there are technological limitations of these approaches to achieving quantitative molecular level information on the structural and biophysical changes resulting from ABPs interaction with F-actin. Fundamental questions about the actin structure and dynamics and how these determine the function of ABPs remain unanswered. Specifically, how local and long-range structural and conformational changes result in ABPs induced remodeling of F-actin needs to be addressed at the single filament level. Advanced, sensitive and accurate experimental tools for detailed understanding of ABP–actin interactions are much needed. This article discusses the current understanding of nanoscale structural and mechanical modulation of F-actin by ABPs at the single filament level using several correlative microscopic techniques, focusing mainly on results obtained by Atomic Force Microscopy (AFM) analysis of ABP–actin complexes.

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Conformational dynamics of actin: Effectors and implications for biological function

Cited by 44 publications

References 275 publications

Mitochondrial dysfunction and mitochondrial dynamics-The cancer connection

Mitochondrial dysfunction and mitochondrial dynamics-The cancer connection

MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation

Correlative nanoscale imaging of actin filaments and their complexes

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