Myosin-II-Dependent Localization and Dynamics of F-Actin during Cytokinesis

Murthy, Kausalya; Wadsworth, Patricia

doi:10.1016/j.cub.2005.04.048

Cited by 47 publications

(68 citation statements)

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“…2b and 2c). In addition, comparison of the rates of cortical flow (which is slowed when actin dynamics are reduced or myosin-2-dependent contraction is inhibited) [Mandato and Bement, 2001;Murthy and Wadsworth, 2005] revealed no significant differences between the four groups (Fig. 2d).…”

Section: Utrch-based Probes For Imaging F-actin In Living Cellsmentioning

confidence: 90%

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Versatile fluorescent probes for actin filaments based on the actin‐binding domain of utrophin

Burkel

Dassow

Bement

2007

Cell Motil. Cytoskeleton

452

485

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Actin filaments (F-actin) are protein polymers that undergo rapid assembly and disassembly and control an enormous variety of cellular processes ranging from force production to regulation of signal transduction. Consequently, imaging of F-actin has become an increasingly important goal for biologists seeking to understand how cells and tissues function. However, most of the available means for imaging F-actin in living cells suffer from one or more biological or experimental shortcomings. Here we describe fluorescent F-actin probes based on the calponin homology domain of utrophin (Utr-CH), which binds F-actin without stabilizing it in vitro. We show that these probes faithfully report the distribution of F-actin in living and fixed cells, distinguish between stable and dynamic F-actin, and have no obvious effects on processes that depend critically on the balance of actin assembly and disassembly.

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Section: Utrch-based Probes For Imaging F-actin In Living Cellsmentioning

confidence: 90%

“…5e and 5f) regions in control oocytes vs. oocytes treated with jasplakinolide, which stabilizes F-actin [e.g. Murthy and Wadsworth, 2005]. In both cases, jasplakinolide greatly reduced the rate of PaGFP-UtrCH probe decay after photoactivation (Figs.…”

Section: Distinguishing Between Stable and Dynamic Actin In Living Cellsmentioning

confidence: 97%

Versatile fluorescent probes for actin filaments based on the actin‐binding domain of utrophin

Burkel

Dassow

Bement

2007

Cell Motil. Cytoskeleton

452

485

View full text Add to dashboard Cite

show abstract

“…We then investigated if this low myosin accumulation in the contractile ring was capable to generate a myosin activity. Activation of myosin II was assessed by exploring the phosphorylation status of its regulatory light chain (MLC2) with an antibody recognizing PPMLC2-, Ser 19 and Thr 18 -phosphorylated forms of MLC2. A positive signal was easily seen at late telophase in 68.6% (n = 102, three independent experiments) of dipolar mitotic/endomitotic MK with a cleavage furrow ≥75% cell transversal diameter (Fig.…”

Section: Myh10 Is Involved In Mk Ploidy Regulationmentioning

confidence: 99%

“…This experiment indicates that there still exists some myosin II activity at the contractile ring at the end of MK telophase, even with a reduced myosin heavy chain accumulation. MLC2 phosphorylation regulates myosin II activity without affecting the recruitment of myosin II and F-actin in the contractile ring 13,17,18 and controls the actin dynamics (assembly and disassembly) necessary for completion of cytokinesis 19 . To study actin turnover, CD34 + cells were transfected with a GFP-β-actin construct and induced to differentiate into hematopoietic cells by a cocktail of growth factors.…”

Section: Myh10 Is Involved In Mk Ploidy Regulationmentioning

confidence: 99%

RUNX1-induced silencing of non-muscle myosin heavy chain IIB contributes to megakaryocyte polyploidization

et al. 2012

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megakaryocytes are unique mammalian cells that undergo polyploidization (endomitosis) during differentiation, leading to an increase in cell size and protein production that precedes platelet production. Recent evidence demonstrates that endomitosis is a consequence of a late failure in cytokinesis associated with a contractile ring defect. Here we show that the non-muscle myosin IIB heavy chain (mYH10) is expressed in immature megakaryocytes and specifically localizes in the contractile ring. mYH10 downmodulation by short hairpin RnA increases polyploidization by inhibiting the return of 4n cells to 2n, but other regulators, such as of the G1/s transition, might regulate further polyploidization of the 4n cells. Conversely, re-expression of mYH10 in the megakaryocytes prevents polyploidization and the transition of 2n to 4n cells. During polyploidization, mYH10 expression is repressed by the major megakaryocyte transcription factor RunX1. Thus, RunX1-mediated silencing of mYH10 is required for the switch from mitosis to endomitosis, linking polyploidization with megakaryocyte differentiation.

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“…For example, this force is involved in physiological processes such as cellular migration [4], proliferation [5], and differentiation [6]. The activities of these physiological processes are strongly influenced by external loading forces [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Development of a device to stretch tissue-like materials and to measure their mechanical properties by scanning probe microscopy

2007

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We developed a new stretch device to investigate the biomechanical responses to an external loading force on a tissue-like material consisting of cells and a collagen gel. Collagen gel, a typical matrix found abundantly in the connective tissue, was attached to an elastic chamber that was precoated with a thin layer of collagen. Madin-Darby canine kidney (MDCK) cells that were cultured on the collagen gel were stretched in a uniaxial direction via deformation of the elastic chamber. Changes in the morphology and stiffness of the tissue-like structure were measured before and after the stretch by using wide-range scanning probe microscopy (WR-SPM). The change in cellular morphology was heterogeneous, and there was a 2-fold increase in the intercellular junction due to the stretch. In addition to the SPM measurements, this device enables observation of the spatial distribution of cytoskeletal proteins such as vimentin and α-catenin by using immunofluorescent microscopy. We concluded that the stretch device we have reported in this paper is useful to measure the mechanical response of a tissue-like material over a range of cell sizes when exposed to an external loading force.

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Myosin-II-Dependent Localization and Dynamics of F-Actin during Cytokinesis

Cited by 47 publications

References 0 publications

Versatile fluorescent probes for actin filaments based on the actin‐binding domain of utrophin

Versatile fluorescent probes for actin filaments based on the actin‐binding domain of utrophin

RUNX1-induced silencing of non-muscle myosin heavy chain IIB contributes to megakaryocyte polyploidization

Development of a device to stretch tissue-like materials and to measure their mechanical properties by scanning probe microscopy

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