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  1. Article ; Online: A mechanosensory system controls cell shape changes during mitosis.

    Effler, Janet C / Iglesias, Pablo A / Robinson, Douglas N

    Cell cycle (Georgetown, Tex.)

    2007  Volume 6, Issue 1, Page(s) 30–35

    Abstract: Essential life processes are heavily controlled by a variety of positive and negative feedback systems. Cytokinesis failure, ultimately leading to aneuploidy, is appreciated as an early step in tumor formation in mammals and is deleterious for all cells. ...

    Abstract Essential life processes are heavily controlled by a variety of positive and negative feedback systems. Cytokinesis failure, ultimately leading to aneuploidy, is appreciated as an early step in tumor formation in mammals and is deleterious for all cells. Further, the growing list of cancer predisposition mutations includes a number of genes whose proteins control mitosis and/or cytokinesis. Cytokinesis shape control is also an important part of pattern formation and cell-type specialization during multi-cellular development. Inherently mechanical, we hypothesized that mechanosensing and mechanical feedback are fundamental for cytokinesis shape regulation. Using mechanical perturbation, we identified a mechanosensory control system that monitors shape progression during cytokinesis. In this review, we summarize these findings and their implications for cytokinesis regulation and for understanding the cytoskeletal system architecture that governs shape control.
    MeSH term(s) Animals ; Cell Shape/physiology ; Cytokinesis/physiology ; Humans ; Mechanoreceptors/physiology ; Mechanotransduction, Cellular/physiology ; Mitosis/physiology
    Language English
    Publishing date 2007-01-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.4161/cc.6.1.3674
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  2. Article: Enlazin, a natural fusion of two classes of canonical cytoskeletal proteins, contributes to cytokinesis dynamics.

    Octtaviani, Edelyn / Effler, Janet C / Robinson, Douglas N

    Molecular biology of the cell

    2006  Volume 17, Issue 12, Page(s) 5275–5286

    Abstract: Cytokinesis requires a complex network of equatorial and global proteins to regulate cell shape changes. Here, using interaction genetics, we report the first characterization of a novel protein, enlazin. Enlazin is a natural fusion of two canonical ... ...

    Abstract Cytokinesis requires a complex network of equatorial and global proteins to regulate cell shape changes. Here, using interaction genetics, we report the first characterization of a novel protein, enlazin. Enlazin is a natural fusion of two canonical classes of actin-associated proteins, the ezrin-radixin-moesin family and fimbrin, and it is localized to actin-rich structures. A fragment of enlazin, enl-tr, was isolated as a genetic suppressor of the cytokinesis defect of cortexillin-I mutants. Expression of enl-tr disrupts expression of endogenous enlazin, indicating that enl-tr functions as a dominant-negative lesion. Enlazin is distributed globally during cytokinesis and is required for cortical tension and cell adhesion. Consistent with a role in cell mechanics, inhibition of enlazin in a cortexillin-I background restores cytokinesis furrowing dynamics and suppresses the growth-in-suspension defect. However, as expected for a role in cell adhesion, inhibiting enlazin in a myosin-II background induces a synthetic cytokinesis phenotype, frequently arresting furrow ingression at the dumbbell shape and/or causing recession of the furrow. Thus, enlazin has roles in cell mechanics and adhesion, and these roles seem to be differentially significant for cytokinesis, depending on the genetic background.
    MeSH term(s) Amino Acid Sequence ; Animals ; Biomechanical Phenomena ; Cell Adhesion ; Cell Growth Processes ; Cytokinesis ; Cytoskeletal Proteins/metabolism ; Dictyostelium/cytology ; Dictyostelium/metabolism ; Gene Silencing ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Mutation/genetics ; Peptide Fragments/metabolism ; Phenotype ; Protozoan Proteins/chemistry ; Protozoan Proteins/metabolism
    Chemical Substances Cytoskeletal Proteins ; Microfilament Proteins ; Peptide Fragments ; Protozoan Proteins ; ctxA protein, Dictyostelium discoideum
    Language English
    Publishing date 2006-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E06-08-0767
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  3. Article: The stress and strain of cytokinesis.

    Reichl, Elizabeth M / Effler, Janet C / Robinson, Douglas N

    Trends in cell biology

    2005  Volume 15, Issue 4, Page(s) 200–206

    Abstract: The ultimate goal of all signaling pathways in cytokinesis is to control the mechanical separation of the mother cell into two daughter cells. Because of the intrinsic mechanical nature of cytokinesis, it is essential to understand fully how cell shapes ... ...

    Abstract The ultimate goal of all signaling pathways in cytokinesis is to control the mechanical separation of the mother cell into two daughter cells. Because of the intrinsic mechanical nature of cytokinesis, it is essential to understand fully how cell shapes and the material properties of the cell are generated, how these shapes and material properties create force, and how motor proteins such as myosin-II modify the system to achieve successful cytokinesis. In this review (which is part of the Cytokinesis series), we discuss the relevant physical properties of cells, how these properties are measured and the basic models that are used to understand cell mechanics. Finally, we present our current understanding of how cytokinesis mechanics work.
    MeSH term(s) Biomechanical Phenomena ; Cell Division ; Cytokinesis ; Microscopy, Atomic Force ; Models, Biological ; Signal Transduction
    Language English
    Publishing date 2005-01-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2005.02.004
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  4. Article ; Online: Mechanosensing through cooperative interactions between myosin II and the actin crosslinker cortexillin I.

    Ren, Yixin / Effler, Janet C / Norstrom, Melanie / Luo, Tianzhi / Firtel, Richard A / Iglesias, Pablo A / Rock, Ronald S / Robinson, Douglas N

    Current biology : CB

    2009  Volume 19, Issue 17, Page(s) 1421–1428

    Abstract: Background: Mechanosensing governs many processes from molecular to organismal levels, including during cytokinesis where it ensures successful and symmetrical cell division. Although many proteins are now known to be force sensitive, myosin motors with ...

    Abstract Background: Mechanosensing governs many processes from molecular to organismal levels, including during cytokinesis where it ensures successful and symmetrical cell division. Although many proteins are now known to be force sensitive, myosin motors with their ATPase activity and force-sensitive mechanical steps are well poised to facilitate cellular mechanosensing. For a myosin motor to experience tension, the actin filament must also be anchored.
    Results: Here, we find a cooperative relationship between myosin II and the actin crosslinker cortexillin I where both proteins are essential for cellular mechanosensory responses. Although many functions of cortexillin I and myosin II are dispensable for cytokinesis, all are required for full mechanosensing. Our analysis demonstrates that this mechanosensor has three critical elements: the myosin motor where the lever arm acts as a force amplifier, a force-sensitive bipolar thick-filament assembly, and a long-lived actin crosslinker, which anchors the actin filament so that the motor may experience tension. We also demonstrate that a Rac small GTPase inhibits this mechanosensory module during interphase, allowing the module to be primarily active during cytokinesis.
    Conclusions: Overall, myosin II and cortexillin I define a cellular-scale mechanosensor that controls cell shape during cytokinesis. This system is exquisitely tuned through the enzymatic properties of the myosin motor, its lever arm length, and bipolar thick-filament assembly dynamics. The system also requires cortexillin I to stably anchor the actin filament so that the myosin motor can experience tension. Through this cross-talk, myosin II and cortexillin I define a cellular-scale mechanosensor that monitors and corrects shape defects, ensuring symmetrical cell division.
    MeSH term(s) Dictyostelium/cytology ; Dictyostelium/physiology ; Mechanotransduction, Cellular/physiology ; Microfilament Proteins/metabolism ; Microfilament Proteins/physiology ; Models, Biological ; Myosin Type II/metabolism ; Myosin Type II/physiology ; Phosphorylation ; Protozoan Proteins/metabolism ; Protozoan Proteins/physiology ; rac GTP-Binding Proteins/metabolism ; rac GTP-Binding Proteins/physiology
    Chemical Substances Microfilament Proteins ; Protozoan Proteins ; RacE protein, Dictyostelium discoideum ; ctxA protein, Dictyostelium discoideum ; Myosin Type II (EC 3.6.1.-) ; rac GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2009-07-30
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2009.07.018
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  5. Article ; Online: Modeling cellular deformations using the level set formalism.

    Yang, Liu / Effler, Janet C / Kutscher, Brett L / Sullivan, Sarah E / Robinson, Douglas N / Iglesias, Pablo A

    BMC systems biology

    2008  Volume 2, Page(s) 68

    Abstract: Background: Many cellular processes involve substantial shape changes. Traditional simulations of these cell shape changes require that grids and boundaries be moved as the cell's shape evolves. Here we demonstrate that accurate cell shape changes can ... ...

    Abstract Background: Many cellular processes involve substantial shape changes. Traditional simulations of these cell shape changes require that grids and boundaries be moved as the cell's shape evolves. Here we demonstrate that accurate cell shape changes can be recreated using level set methods (LSM), in which the cellular shape is defined implicitly, thereby eschewing the need for updating boundaries.
    Results: We obtain a viscoelastic model of Dictyostelium cells using micropipette aspiration and show how this viscoelastic model can be incorporated into LSM simulations to recreate the observed protrusion of cells into the micropipette faithfully. We also demonstrate the use of our techniques by simulating the cell shape changes elicited by the chemotactic response to an external chemoattractant gradient.
    Conclusion: Our results provide a simple but effective means of incorporating cellular deformations into mathematical simulations of cell signaling. Such methods will be useful for simulating important cellular events such as chemotaxis and cytokinesis.
    MeSH term(s) Animals ; Biomechanical Phenomena ; Cell Membrane/metabolism ; Cell Shape ; Cell Size ; Chemotaxis ; Cytoskeleton/metabolism ; Dictyostelium/cytology ; Elasticity ; Models, Biological ; Pressure ; Sensitivity and Specificity ; Viscosity
    Language English
    Publishing date 2008-07-24
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1752-0509
    ISSN (online) 1752-0509
    DOI 10.1186/1752-0509-2-68
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  6. Article: Antibody to dengue 1 detected more than 60 years after infection.

    Imrie, Allison / Meeks, Janet / Gurary, Alexandra / Sukhbaatar, Munkhzul / Truong, Thang Thua / Cropp, C Bruce / Effler, Paul

    Viral immunology

    2008  Volume 20, Issue 4, Page(s) 672–675

    Abstract: We investigated the duration of humoral responses to dengue virus infection in individuals who recalled experiencing dengue fever-like illnesses at the time of the Second World War, when dengue fever epidemics occurred throughout the Pacific and ... ...

    Abstract We investigated the duration of humoral responses to dengue virus infection in individuals who recalled experiencing dengue fever-like illnesses at the time of the Second World War, when dengue fever epidemics occurred throughout the Pacific and Southeast Asia. In July 1943 dengue fever reappeared in Hawaii following an interval of 31 years. Over the next 12 months a total of 1498 locally transmitted cases were reported, and at least 46 imported cases were identified, most of which were among members of the military returning from the Pacific Theatre of the war. Serum samples collected in 2005, more than 60 years after onset of symptoms, were tested for the presence of dengue-specific antibodies using a rapid ELISA test, and by plaque reduction neutralization test. Four of seven samples were positive for dengue-specific IgG and demonstrated neutralization titers >or=160 to dengue 1. We describe the existence of dengue-specific antibodies in the serum of people infected more than 60 years earlier.
    MeSH term(s) Aged ; Aged, 80 and over ; Animals ; Antibodies, Viral/blood ; Antibodies, Viral/immunology ; Dengue/epidemiology ; Dengue/immunology ; Dengue Virus/immunology ; Dengue Virus/pathogenicity ; Disease Outbreaks ; Enzyme-Linked Immunosorbent Assay/methods ; Female ; Hawaii/epidemiology ; Humans ; Immunoglobulin G/blood ; Immunoglobulin G/immunology ; Male ; Neutralization Tests ; Pacific Islands/epidemiology
    Chemical Substances Antibodies, Viral ; Immunoglobulin G
    Language English
    Publishing date 2008-08-13
    Publishing country United States
    Document type Case Reports ; Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 639075-4
    ISSN 1557-8976 ; 0882-8245
    ISSN (online) 1557-8976
    ISSN 0882-8245
    DOI 10.1089/vim.2007.0050
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  7. Article ; Online: Modeling cellular deformations using the level set formalism

    Yang Liu / Effler Janet C / Kutscher Brett L / Sullivan Sarah E / Robinson Douglas N / Iglesias Pablo A

    BMC Systems Biology, Vol 2, Iss 1, p

    2008  Volume 68

    Abstract: Abstract Background Many cellular processes involve substantial shape changes. Traditional simulations of these cell shape changes require that grids and boundaries be moved as the cell's shape evolves. Here we demonstrate that accurate cell shape ... ...

    Abstract Abstract Background Many cellular processes involve substantial shape changes. Traditional simulations of these cell shape changes require that grids and boundaries be moved as the cell's shape evolves. Here we demonstrate that accurate cell shape changes can be recreated using level set methods (LSM), in which the cellular shape is defined implicitly, thereby eschewing the need for updating boundaries. Results We obtain a viscoelastic model of Dictyostelium cells using micropipette aspiration and show how this viscoelastic model can be incorporated into LSM simulations to recreate the observed protrusion of cells into the micropipette faithfully. We also demonstrate the use of our techniques by simulating the cell shape changes elicited by the chemotactic response to an external chemoattractant gradient. Conclusion Our results provide a simple but effective means of incorporating cellular deformations into mathematical simulations of cell signaling. Such methods will be useful for simulating important cellular events such as chemotaxis and cytokinesis.
    Keywords Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2008-07-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
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  8. Article: Mitosis-specific mechanosensing and contractile-protein redistribution control cell shape.

    Effler, Janet C / Kee, Yee-Seir / Berk, Jason M / Tran, Minhchau N / Iglesias, Pablo A / Robinson, Douglas N

    Current biology : CB

    2006  Volume 16, Issue 19, Page(s) 1962–1967

    Abstract: Because cell-division failure is deleterious, promoting tumorigenesis in mammals, cells utilize numerous mechanisms to control their cell-cycle progression. Though cell division is considered a well-ordered sequence of biochemical events, cytokinesis, an ...

    Abstract Because cell-division failure is deleterious, promoting tumorigenesis in mammals, cells utilize numerous mechanisms to control their cell-cycle progression. Though cell division is considered a well-ordered sequence of biochemical events, cytokinesis, an inherently mechanical process, must also be mechanically controlled to ensure that two equivalent daughter cells are produced with high fidelity. Given that cells respond to their mechanical environment, we hypothesized that cells utilize mechanosensing and mechanical feedback to sense and correct shape asymmetries during cytokinesis. Because the mitotic spindle and myosin II are vital to cell division, we explored their roles in responding to shape perturbations during cell division. We demonstrate that the contractile proteins myosin II and cortexillin I redistribute in response to intrinsic and externally induced shape asymmetries. In early cytokinesis, mechanical load overrides spindle cues and slows cytokinesis progression while contractile proteins accumulate and correct shape asymmetries. In late cytokinesis, mechanical perturbation also directs contractile proteins but without apparently disrupting cytokinesis. Significantly, this response only occurs during anaphase through cytokinesis, does not require microtubules, and is independent of spindle orientation, but is dependent on myosin II. Our data provide evidence for a mechanosensory system that directs contractile proteins to regulate cell shape during mitosis.
    MeSH term(s) Animals ; Cell Shape ; Dictyostelium/cytology ; Dictyostelium/metabolism ; Dictyostelium/ultrastructure ; Mechanotransduction, Cellular/physiology ; Microfilament Proteins/analysis ; Microfilament Proteins/metabolism ; Microfilament Proteins/physiology ; Mitosis/physiology ; Models, Biological ; Myosin Type II/analysis ; Myosin Type II/metabolism ; Myosin Type II/physiology ; Protozoan Proteins/analysis ; Protozoan Proteins/metabolism ; Protozoan Proteins/physiology ; Spindle Apparatus/physiology ; Spindle Apparatus/ultrastructure
    Chemical Substances Microfilament Proteins ; Protozoan Proteins ; ctxA protein, Dictyostelium discoideum ; Myosin Type II (EC 3.6.1.-)
    Language English
    Publishing date 2006-10-10
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2006.08.027
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  9. Article: Interactions between myosin and actin crosslinkers control cytokinesis contractility dynamics and mechanics.

    Reichl, Elizabeth M / Ren, Yixin / Morphew, Mary K / Delannoy, Michael / Effler, Janet C / Girard, Kristine D / Divi, Srikanth / Iglesias, Pablo A / Kuo, Scot C / Robinson, Douglas N

    Current biology : CB

    2008  Volume 18, Issue 7, Page(s) 471–480

    Abstract: Introduction: Contractile networks are fundamental to many cellular functions, particularly cytokinesis and cell motility. Contractile networks depend on myosin-II mechanochemistry to generate sliding force on the actin polymers. However, to be ... ...

    Abstract Introduction: Contractile networks are fundamental to many cellular functions, particularly cytokinesis and cell motility. Contractile networks depend on myosin-II mechanochemistry to generate sliding force on the actin polymers. However, to be contractile, the networks must also be crosslinked by crosslinking proteins, and to change the shape of the cell, the network must be linked to the plasma membrane. Discerning how this integrated network operates is essential for understanding cytokinesis contractility and shape control. Here, we analyzed the cytoskeletal network that drives furrow ingression in Dictyostelium.
    Results: We establish that the actin polymers are assembled into a meshwork and that myosin-II does not assemble into a discrete ring in the Dictyostelium cleavage furrow of adherent cells. We show that myosin-II generates regional mechanics by increasing cleavage furrow stiffness and slows furrow ingression during late cytokinesis as compared to myoII nulls. Actin crosslinkers dynacortin and fimbrin similarly slow furrow ingression and contribute to cell mechanics in a myosin-II-dependent manner. By using FRAP, we show that the actin crosslinkers have slower kinetics in the cleavage furrow cortex than in the pole, that their kinetics differ between wild-type and myoII null cells, and that the protein dynamics of each crosslinker correlate with its impact on cortical mechanics.
    Conclusions: These observations suggest that myosin-II along with actin crosslinkers establish local cortical tension and elasticity, allowing for contractility independent of a circumferential cytoskeletal array. Furthermore, myosin-II and actin crosslinkers may influence each other as they modulate the dynamics and mechanics of cell-shape change.
    MeSH term(s) Actins/metabolism ; Animals ; Biomechanical Phenomena ; Cytokinesis/physiology ; Dictyostelium/physiology ; Myosin Type II/physiology
    Chemical Substances Actins ; Myosin Type II (EC 3.6.1.-)
    Language English
    Publishing date 2008-03-27
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2008.02.056
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