Faculty Opinions recommendation of ZIP kinase is responsible for the phosphorylation of myosin II and necessary for cell motility in mammalian fibroblasts.

2004 ◽  
Author(s):  
Martin A Schwartz
Keyword(s):  
Cell Motility ◽  
Myosin Ii

scholarly journals The distribution of myosin II in Dictyostelium discoideum slug cells.

1991 ◽  
Vol 115 (5) ◽  
pp. 1267-1274 ◽  
Author(s):  
S Eliott ◽  
P H Vardy ◽  
K L Williams
Keyword(s):  
Cell Motility ◽  
Dictyostelium Discoideum ◽  
Immunofluorescence Microscopy ◽  
Molecular Genetic ◽  
Myosin Ii ◽  
Three Dimensional ◽  
Homogeneous Distribution ◽  
Multicellular Development ◽  
Insight Into

While the role of myosin II in muscle contraction has been well characterized, less is known about the role of myosin II in non-muscle cells. Recent molecular genetic experiments on Dictyostelium discoideum show that myosin II is necessary for cytokinesis and multicellular development. Here we use immunofluorescence microscopy with monoclonal and polyclonal antimyosin antibodies to visualize myosin II in cells of the multicellular D. discoideum slug. A subpopulation of peripheral and anterior cells label brightly with antimyosin II antibodies, and many of these cells display a polarized intracellular distribution of myosin II. Other cells in the slug label less brightly and their cytoplasm displays a more homogeneous distribution of myosin II. These results provide insight into cell motility within a three-dimensional tissue and they are discussed in relation to the possible roles of myosin II in multicellular development.

scholarly journals Confinement hinders motility by inducing RhoA-mediated nuclear influx, volume expansion, and blebbing

2019 ◽  
Vol 218 (12) ◽  
pp. 4093-4111 ◽  
Author(s):  
Panagiotis Mistriotis ◽  
Emily O. Wisniewski ◽  
Kaustav Bera ◽  
Jeremy Keys ◽  
Yizeng Li ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Cell Motility ◽  
Volume Expansion ◽  
Myosin Ii ◽  
Nuclear Volume ◽  
Linc Complex ◽  
Actomyosin Contractility ◽  
Dependent Pathway ◽  
Passive Influx

Cells migrate in vivo through complex confining microenvironments, which induce significant nuclear deformation that may lead to nuclear blebbing and nuclear envelope rupture. While actomyosin contractility has been implicated in regulating nuclear envelope integrity, the exact mechanism remains unknown. Here, we argue that confinement-induced activation of RhoA/myosin-II contractility, coupled with LINC complex-dependent nuclear anchoring at the cell posterior, locally increases cytoplasmic pressure and promotes passive influx of cytoplasmic constituents into the nucleus without altering nuclear efflux. Elevated nuclear influx is accompanied by nuclear volume expansion, blebbing, and rupture, ultimately resulting in reduced cell motility. Moreover, inhibition of nuclear efflux is sufficient to increase nuclear volume and blebbing on two-dimensional surfaces, and acts synergistically with RhoA/myosin-II contractility to further augment blebbing in confinement. Cumulatively, confinement regulates nuclear size, nuclear integrity, and cell motility by perturbing nuclear flux homeostasis via a RhoA-dependent pathway.

scholarly journals p114RhoGEF governs cell motility and lumen formation during tubulogenesis through a ROCK-myosin-II pathway

2015 ◽  
Vol 128 (23) ◽  
pp. 4317-4327 ◽  
Author(s):  
M. Kim ◽  
A. M. Shewan ◽  
A. J. Ewald ◽  
Z. Werb ◽  
K. E. Mostov
Keyword(s):  
Cell Motility ◽  
Myosin Ii ◽  
Lumen Formation

scholarly journals Rap1 controls cell adhesion and cell motility through the regulation of myosin II

2007 ◽  
Vol 176 (7) ◽  
pp. 1021-1033 ◽  
Author(s):  
Taeck J. Jeon ◽  
Dai-Jen Lee ◽  
Sylvain Merlot ◽  
Gerald Weeks ◽  
Richard A. Firtel
Keyword(s):  
Cell Adhesion ◽  
Cell Motility ◽  
Myosin Ii ◽  
Leading Edge ◽  
In Vitro Assay ◽  
Filamentous Actin ◽  
Guanosine Triphosphate ◽  
Vitro Assay

We have investigated the role of Rap1 in controlling chemotaxis and cell adhesion in Dictyostelium discoideum. Rap1 is activated rapidly in response to chemoattractant stimulation, and activated Rap1 is preferentially found at the leading edge of chemotaxing cells. Cells expressing constitutively active Rap1 are highly adhesive and exhibit strong chemotaxis defects, which are partially caused by an inability to spatially and temporally regulate myosin assembly and disassembly. We demonstrate that the kinase Phg2, a putative Rap1 effector, colocalizes with Rap1–guanosine triphosphate at the leading edge and is required in an in vitro assay for myosin II phosphorylation, which disassembles myosin II and facilitates filamentous actin–mediated leading edge protrusion. We suggest that Rap1/Phg2 plays a role in controlling leading edge myosin II disassembly while passively allowing myosin II assembly along the lateral sides and posterior of the cell.

scholarly journals An increase or a decrease in myosin II phosphorylation inhibits macrophage motility.

1991 ◽  
Vol 114 (2) ◽  
pp. 277-283 ◽  
Author(s):  
A K Wilson ◽  
G Gorgas ◽  
W D Claypool ◽  
P de Lanerolle
Keyword(s):  
Cell Motility ◽  
Light Chain ◽  
Mammalian Cells ◽  
Inverse Relationship ◽  
Myosin Light Chain ◽  
Myosin Ii ◽  
Active Form ◽  
Chemotaxis Assay ◽  
Mlc20 Phosphorylation ◽  
Number Of Cells

Myosin II purified from mammalian non-muscle cells is phosphorylated on the 20-kD light chain subunit (MLC20) by the Ca2+/calmodulin-dependent enzyme myosin light chain kinase (MLCK). The importance of MLC20 phosphorylation in regulating cell motility was investigated by introducing either antibodies to MLCK (MK-Ab) or a Ca2+/calmodulin-independent, constitutively active form of MLCK (MK-) into macrophages. The effects of these proteins on cell motility were then determined using a quantitative chemotaxis assay. Chemotaxis is significantly diminished in macrophages containing MK-Ab compared to macrophages containing control antibodies. Moreover, there is an inverse relationship between the number of cells that migrate and the amount of MK-Ab introduced into cells. Interestingly, there is also an inverse relationship between the number of cells that migrate and the amount of MK- introduced into cells. Other experiments demonstrated that MK-Ab decreased intracellular MLC20 phosphorylation while MK- increased MLC20 phosphorylation. MK- also increased the amount of myosin associated with the cytoskeleton. These data demonstrate that the regulation of MLCK is an important aspect of cell motility and suggest that MLC20 phosphorylation must be maintained within narrow limits during translational motility by mammalian cells.

scholarly journals Self-sorting of nonmuscle myosins IIA and IIB polarizes the cytoskeleton and modulates cell motility

2017 ◽  
Vol 216 (9) ◽  
pp. 2877-2889 ◽  
Author(s):  
Maria S. Shutova ◽  
Sreeja B. Asokan ◽  
Shefali Talwar ◽  
Richard K. Assoian ◽  
James E. Bear ◽  
...  
Keyword(s):  
Cell Motility ◽  
Cell Polarity ◽  
Myosin Ii ◽  
Leading Edge ◽  
Stress Fibers ◽  
Cell Behavior ◽  
Retrograde Flow ◽  
Nonmuscle Myosin ◽  
Cell Contractility ◽  
Nonmuscle Myosin Ii

Nonmuscle myosin II (NMII) is uniquely responsible for cell contractility and thus defines multiple aspects of cell behavior. To generate contraction, NMII molecules polymerize into bipolar minifilaments. Different NMII paralogs are often coexpressed in cells and can copolymerize, suggesting that they may cooperate to facilitate cell motility. However, whether such cooperation exists and how it may work remain unknown. We show that copolymerization of NMIIA and NMIIB followed by their differential turnover leads to self-sorting of NMIIA and NMIIB along the front–rear axis, thus producing a polarized actin–NMII cytoskeleton. Stress fibers newly formed near the leading edge are enriched in NMIIA, but over time, they become progressively enriched with NMIIB because of faster NMIIA turnover. In combination with retrograde flow, this process results in posterior accumulation of more stable NMIIB-rich stress fibers, thus strengthening cell polarity. By copolymerizing with NMIIB, NMIIA accelerates the intrinsically slow NMIIB dynamics, thus increasing cell motility and traction and enabling chemotaxis.

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