Ablation of Nonmuscle Myosin II-B and II-C Reveals a Role for Nonmuscle Myosin II in Cardiac Myocyte Karyokinesis

Ma, Xuefei; Jana, Siddhartha S.; Conti, Mary Anne; Kawamoto, Sachiyo; Claycomb, William C.; Adelstein, Robert S.

doi:10.1091/mbc.e10-04-0293

Cited by 100 publications

(171 citation statements)

References 43 publications

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“…At 96 hours after cells were treated with adenoviral GFP-Cre to delete the floxed exon, the cells showed a complete loss of either MIIA or MIIB protein depending on the targeted ablation (supplementary material Fig. S4); there were no compensatory effects on the levels of the other isoform, as shown previously (Jacobelli et al, 2010;Ma et al, 2010). Migration studies demonstrated that control adenoviral-GFP MEFs could migrate efficiently on 1D substrates, with a 1.7-fold higher velocity than on 2D surfaces (Fig.…”

Section: Differential Regulation Of Myosin II Isoforms a And B In Adhsupporting

confidence: 72%

Microenvironmental control of cell migration: Myosin IIA is required for efficient migration in fibrillar environments through control of cell adhesion dynamics

Doyle

Kutys

Conti

et al. 2012

Journal of Cell Science

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108

100

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SummaryRecent evidence suggests that organization of the extracellular matrix (ECM) into aligned fibrils or fibril-like ECM topographies promotes rapid migration in fibroblasts. However, the mechanisms of cell migration that are altered by these changes in microenvironmental topography remain unknown. Here, using 1D fibrillar migration as a model system for oriented fibrillar 3D matrices, we find that fibroblast leading-edge dynamics are enhanced by 1D fibrillar micropatterns and demonstrate a dependence on the spatial positioning of cell adhesions. Although 1D, 2D and 3D matrix adhesions have similar assembly kinetics, both 1D and 3D adhesions are stabilized for prolonged periods, whereas both paxillin and vinculin show slower turnover rates in 1D adhesions. Moreover, actin in 1D adhesions undergoes slower retrograde flow than the actin that is present in 2D lamellipodia. These data suggest an increase in mechanical coupling between adhesions and protrusive machinery. Experimental reduction of contractility resulted in the loss of 1D adhesion structure and stability, with scattered small and unstable adhesions, and an uncoupling of adhesion protein-integrin stability. Genetic ablation of myosin IIA (MIIA) or myosin IIB (MIIB) isoforms revealed that MIIA is required for efficient migration in restricted environments as well as adhesion maturation, whereas MIIB helps to stabilize adhesions beneath the cell body. These data suggest that restricted cell environments, such as 1D patterns, require cellular contraction through MIIA to enhance adhesion stability and coupling to integrins behind the leading edge. This increase in mechanical coupling allows for greater leading-edge protrusion and rapid cell migration.

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Section: Differential Regulation Of Myosin II Isoforms a And B In Adhsupporting

confidence: 72%

Microenvironmental control of cell migration: Myosin IIA is required for efficient migration in fibrillar environments through control of cell adhesion dynamics

Doyle

Kutys

Conti

et al. 2012

Journal of Cell Science

Self Cite

108

100

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“…However, there is no increase in NMIIA or NMIIC, the former being absent and the later remaining low after birth. Moreover, Nkx2.5-Cre-mediated knockout of NMIIA in cardiac myocytes shows no effect on mouse heart development (Conti et al, 2015) nor does knockout of NMIIC (Ma et al, 2010). The temporal pattern of NMIIB expression in developing cardiac myocytes is consistent with its role in regulating cardiac myocyte proliferation.…”

Section: Nmiib Function In Myocardial Growthmentioning

confidence: 97%

Nonmuscle myosin II-B regulates epicardial integrity and epicardial derived mesenchymal cell maturation

Sung

Yang

et al. 2017

Journal of Cell Science

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Nonmuscle myosin IIB (NMIIB; heavy chain encoded by MYH10) is essential for cardiac myocyte cytokinesis. The role of NMIIB in other cardiac cells is not known. Here, we show that NMIIB is required in epicardial formation and functions to support myocardial proliferation and coronary vessel development. Ablation of NMIIB in epicardial cells results in disruption of epicardial integrity with a loss of E-cadherin at cell-cell junctions and a focal detachment of epicardial cells from the myocardium. NMIIB-knockout and blebbistatin-treated epicardial explants demonstrate impaired mesenchymal cell maturation during epicardial epithelial-mesenchymal transition. This is manifested by an impaired invasion of collagen gels by the epicardium-derived mesenchymal cells and the reorganization of the cytoskeletal structure. Although there is a marked decrease in the expression of mesenchymal genes, there is no change in Snail (also known as Snai1) or E-cadherin expression. Studies from epicardiumspecific NMIIB-knockout mice confirm the importance of NMIIB for epicardial integrity and epicardial functions in promoting cardiac myocyte proliferation and coronary vessel formation during heart development. Our findings provide a novel mechanism linking epicardial formation and epicardial function to the activity of the cytoplasmic motor protein NMIIB.

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“…Cells-To detect proteins that associate with NM II-B, we used COS-7 cells which express NM II-B as the major isoform (92% NM II-B, 8% NM II-C determined by mass spectrometry) (35,36). Using antibodies specific for NMHC II-B, a 180 kDa protein was co-immunoprecipitated with NMHC II-B and separated by SDS-PAGE.…”

Section: Identification Of the Egfr As A Nm Ii-b Binding Partner In Cmentioning

confidence: 99%

Nonmuscle Myosin II Is Required for Internalization of the Epidermal Growth Factor Receptor and Modulation of Downstream Signaling

Kim

Wang

Conti

et al. 2012

Journal of Biological Chemistry

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Background: Cellular internalization of the epidermal growth factor receptor (EGFR) is essential to its downstream signaling. Results: Nonmuscle myosin II (NM II) is required for the internalization of the EGFR and modulates the EGFR-dependent activation of ERK and AKT. Conclusion: NM II binds to the EGFR, expedites internalization and helps to initiate its role in signaling. Significance: These findings elucidate an important step in the function of the EGFR.

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Ablation of Nonmuscle Myosin II-B and II-C Reveals a Role for Nonmuscle Myosin II in Cardiac Myocyte Karyokinesis

Cited by 100 publications

References 43 publications

Microenvironmental control of cell migration: Myosin IIA is required for efficient migration in fibrillar environments through control of cell adhesion dynamics

Microenvironmental control of cell migration: Myosin IIA is required for efficient migration in fibrillar environments through control of cell adhesion dynamics

Nonmuscle myosin II-B regulates epicardial integrity and epicardial derived mesenchymal cell maturation

Nonmuscle Myosin II Is Required for Internalization of the Epidermal Growth Factor Receptor and Modulation of Downstream Signaling

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