New twists in actin–microtubule interactions

Pimm, Morgan L; Henty-Ridilla, Jessica L.

doi:10.1091/mbc.e19-09-0491

Cited by 53 publications

(58 citation statements)

References 125 publications

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“…While intermediate filaments self-assemble, the polymerization of actin and tubulin (microtubule) filaments requires energy and is regulated on multiple levels (Pollard and Goldman, 2018). Importantly, actin and tubulin networks are interlinked (Mohan and John, 2015;Pimm and Henty-Ridilla, 2021). Moreover, actin and/or microtubule cytoskeletons are connected to the nuclear lamina, an intermediate filament network that subtends the nuclear envelope, through a multiprotein LINC complex that spans the nuclear membrane and influences DNA position (Chang et al, 2015;Kim et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Cytoskeleton integrity influences XRCC1 and PCNA dynamics at DNA damage

Hurst

Challa

Shimada

et al. 2021

MBoC

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Upon induction of DNA damage with 405 nm laser light, proteins involved in Base Excision Repair (BER) are recruited to DNA lesions. We find that the dynamics of factors typical of either short-patch (XRCC1) or long-patch (PCNA) BER are altered by chemicals that perturb actin or tubulin polymerization in human cells. Whereas the destabilization of actin filaments by Latrunculin B, Cytochalasin B or Jasplakinolide decreases BER factor accumulation at laser-induced damage, inhibition of tubulin polymerization by Nocodazole increases it. We detect no recruitment of actin to sites of laser-induced DNA damage, yet the depolymerization of cytoplasmic actin filaments elevates both actin and tubulin signals in the nucleus. While published evidence suggested a positive role for F-actin in double-strand break repair in mammals, the enrichment of actin in budding yeast nuclei interferes with BER, augmenting sensitivity to Zeocin. Our quantitative imaging results suggest that the depolymerization of cytoplasmic actin may compromise BER efficiency in mammals not only due to elevated levels of nuclear actin, but also of tubulin. Our study is one of few linking cytoskeletal integrity to BER. [Media: see text] [Media: see text]

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Section: Introductionmentioning

confidence: 99%

Cytoskeleton integrity influences XRCC1 and PCNA dynamics at DNA damage

Hurst

Challa

Shimada

et al. 2021

MBoC

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“…(Huxley, 2004; Mandato, Benink, & Bement, 2000) Further, traditionally, the MT and actin cytoskeleton have been evaluated separately in in vitro assays. Yet, it is becoming clear that actin‐MT crosstalk should be evaluated more ardently with increasing evidence of direct, coordinated relationships, and OT cytoskeletal hierarchical assays provide a unique platform to investigate the synergy of the molecular linkages that connect these structurally distinct filaments (Dogterom & Koenderink, 2019; Even‐Ram et al, 2007; Mandato et al, 2000; Pimm & Henty‐Ridilla, 2021). MTs consist of multiple protofilaments that form a tube and have a higher persistence length than helical AFs (Sept, Baker, & McCammon, 2009; Steffen, Smith, Simmons, & Sleep, 2001).…”

Section: Discussionmentioning

confidence: 99%

Measuring force generation within reconstituted microtubule bundle assemblies using optical tweezers

2021

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Kinesins and microtubule associated proteins (MAPs) are critical to sustain life, facilitating cargo transport, cell division, and motility. To interrogate the mechanistic underpinnings of their function, these microtubule‐based motors and proteins have been studied extensively at the single molecule level. However, a long‐standing issue in the single molecule biophysics field has been how to investigate motors and associated proteins within a physiologically relevant environment in vitro. While the one motor/one filament orientation of a traditional optical trapping assay has revolutionized our knowledge of motor protein mechanics, this reductionist geometry does not reflect the structural hierarchy in which many motors work within the cellular environment. Here, we review approaches that combine the precision of optical tweezers with reconstituted ensemble systems of microtubules, MAPs, and kinesins to understand how each of these unique elements work together to perform large scale cellular tasks, such as but not limited to building the mitotic spindle. Not only did these studies develop novel techniques for investigating motor proteins in vitro, but they also illuminate ensemble filament and motor synergy that helps bridge the mechanistic knowledge gap between previous single molecule and cell level studies.

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“…Tau and MAP2 also facilitate F-actin bundling and cross-linking, microtubule and F-actin crosstalk, neurite growth [ 122 , 123 , 124 , 125 , 126 , 127 , 128 , 129 ], and reduction of these MAPs and pNFHs at the cell periphery predicts inhibition of peripheral F-actin structure, which may facilitate cell shrinkage and a more globular and microtubule-dominated phenotype. We argue that the above patterns facilitate arrest of protrusions and synaptic contacts while maintaining core somatic intracellular structure, and that these adaptations may be present in anoxic turtles.…”

Section: Cytoskeletal Shrinkage In Overwintering Animalsmentioning

confidence: 99%

Cytoskeletal Arrest: An Anoxia Tolerance Mechanism

Myrka

Buck

2021

Metabolites

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Polymerization of actin filaments and microtubules constitutes a ubiquitous demand for cellular adenosine-5′-triphosphate (ATP) and guanosine-5′-triphosphate (GTP). In anoxia-tolerant animals, ATP consumption is minimized during overwintering conditions, but little is known about the role of cell structure in anoxia tolerance. Studies of overwintering mammals have revealed that microtubule stability in neurites is reduced at low temperature, resulting in withdrawal of neurites and reduced abundance of excitatory synapses. Literature for turtles is consistent with a similar downregulation of peripheral cytoskeletal activity in brain and liver during anoxic overwintering. Downregulation of actin dynamics, as well as modification to microtubule organization, may play vital roles in facilitating anoxia tolerance. Mitochondrial calcium release occurs during anoxia in turtle neurons, and subsequent activation of calcium-binding proteins likely regulates cytoskeletal stability. Production of reactive oxygen species (ROS) formation can lead to catastrophic cytoskeletal damage during overwintering and ROS production can be regulated by the dynamics of mitochondrial interconnectivity. Therefore, suppression of ROS formation is likely an important aspect of cytoskeletal arrest. Furthermore, gasotransmitters can regulate ROS levels, as well as cytoskeletal contractility and rearrangement. In this review we will explore the energetic costs of cytoskeletal activity, the cellular mechanisms regulating it, and the potential for cytoskeletal arrest being an important mechanism permitting long-term anoxia survival in anoxia-tolerant species, such as the western painted turtle and goldfish.

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New twists in actin–microtubule interactions

Cited by 53 publications

References 125 publications

Cytoskeleton integrity influences XRCC1 and PCNA dynamics at DNA damage

Cytoskeleton integrity influences XRCC1 and PCNA dynamics at DNA damage

Measuring force generation within reconstituted microtubule bundle assemblies using optical tweezers

Cytoskeletal Arrest: An Anoxia Tolerance Mechanism

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