Kinesin‐5 in Drosophila embryo mitosis: Sliding filament or spindle matrix mechanism?

Scholey, Jonathan M.

doi:10.1002/cm.20349

Cited by 21 publications

(22 citation statements)

References 55 publications

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“…Recent studies have resolved key aspects of the structure and functionality of kinesin-12 (Drechsler et al, 2014;Klejnot et al, 2014), with the idea that interfering with kinesin-12 function could be exploited for cancer therapy. In previous studies, kinesin-12 was found to promote bipolar spindle formation by cooperating with kinesin-5 (also called Eg5 or Kif11), a tetrameric motor protein important for cell division (Kashina et al, 1996;Scholey, 2009;Ferenz et al, 2010). These studies revealed that kinesin-12 is not required for spindle bipolarity in cells with full Eg5 activity but becomes essential when Eg5 is partially inhibited (Tanenbaum et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Depletion of kinesin-12, a myosin-IIB-interacting protein, promotes migration of cortical astrocytes

Feng

Chen

et al. 2016

Journal of Cell Science

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Kinesin-12 (also named Kif15) participates in important events during neuronal development, such as cell division of neuronal precursors, migration of young neurons and establishment of axons and dendritic arbors, by regulating microtubule organization. Little is known about the molecular mechanisms behind the functions of kinesin-12, and even less is known about its roles in other cell types of the nervous system. Here, we show that kinesin-12 depletion from cultured rat cortical astrocytes decreases cell proliferation but increases migration. Co-immunoprecipitation, GST pulldown and small interfering RNA (siRNA) experiments indicated that kinesin-12 directly interacts with myosin-IIB through their tail domains. Immunofluorescence analyses indicated that kinesin-12 and myosin-IIB colocalize in the lamellar region of astrocytes, and fluorescence resonance energy transfer analyses revealed an interaction between the two. The phosphorylation at Thr1142 of kinesin-12 was vital for their interaction. Loss of their interaction through expression of a phosphorylation mutant of kinesin-12 promoted astrocyte migration. We suggest that kinesin-12 and myosin-IIB can form a hetero-oligomer that generates force to integrate microtubules and actin filaments in certain regions of cells, and in the case of astrocytes, that this interaction can modulate their migration.

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Section: Introductionmentioning

confidence: 99%

Depletion of kinesin-12, a myosin-IIB-interacting protein, promotes migration of cortical astrocytes

Feng

Chen

et al. 2016

Journal of Cell Science

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“…Microtubules and actin play a key role in maintaining an ordered pattern and in driving motion (12). Possible force generators during interphase are Kinesin-5 motors between overlapping microtubules, direct active interactions of astral microtubules with nuclei, or active interaction of microtubules with the actin caps via dyneindynactin complexes (13,14).…”

Section: Introductionmentioning

confidence: 99%

The Mechanical Properties of Early Drosophila Embryos Measured by High-Speed Video Microrheology

Wessel

Gumalla

Großhans

et al. 2015

Biophysical Journal

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In early development, Drosophila melanogaster embryos form a syncytium, i.e., multiplying nuclei are not yet separated by cell membranes, but are interconnected by cytoskeletal polymer networks consisting of actin and microtubules. Between division cycles 9 and 13, nuclei and cytoskeleton form a two-dimensional cortical layer. To probe the mechanical properties and dynamics of this self-organizing pre-tissue, we measured shear moduli in the embryo by high-speed video microrheology. We recorded position fluctuations of injected micron-sized fluorescent beads with kHz sampling frequencies and characterized the viscoelasticity of the embryo in different locations. Thermal fluctuations dominated over nonequilibrium activity for frequencies between 0.3 and 1000 Hz. Between the nuclear layer and the yolk, the cytoplasm was homogeneous and viscously dominated, with a viscosity three orders of magnitude higher than that of water. Within the nuclear layer we found an increase of the elastic and viscous moduli consistent with an increased microtubule density. Drug-interference experiments showed that microtubules contribute to the measured viscoelasticity inside the embryo whereas actin only plays a minor role in the regions outside of the actin caps that are closely associated with the nuclei. Measurements at different stages of the nuclear division cycle showed little variation.

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“…Alternatively, the movement might be caused by a dedicated mechanism, and possibly be motor-driven, much like microtubule-microtubule sliding in the mitotic spindle. Microtubule sliding by the plus-end-directed kinesin motor Klp61F (7,8), the minus-end-directed kinesin Ncd (9), and the minus-end-directed cytoplasmic dynein motor (9) are required for proper spindle separation during anaphase. However, Klp61F and Ncd activity is limited to mitosis (10,11).…”

mentioning

confidence: 99%

Kinesin-1 heavy chain mediates microtubule sliding to drive changes in cell shape

Jolly

Kim

Srinivasan

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

124

142

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Microtubules are typically observed to buckle and loop during interphase in cultured cells by an unknown mechanism. We show that lateral microtubule movement and looping is a result of microtubules sliding against one another in interphase Drosophila S2 cells. RNAi of the kinesin-1 heavy chain (KHC), but not dynein or the kinesin-1 light chain, eliminates these movements. KHC-dependent microtubule sliding powers the formation of cellular processes filled with parallel microtubule bundles. The growth of these cellular processes is independent of the actin cytoskeleton. We further observe cytoplasmic microtubule sliding in Xenopus and Ptk2 cells, and show that antibody inhibition of KHC in mammalian cells prevents sliding. We therefore propose that, in addition to its well established role in organelle transport, an important universal function of kinesin-1 is to mediate cytoplasmic microtubule-microtubule sliding. This provides the cell with a dedicated mechanism to transport long and short microtubule filaments and drive changes in cell shape.cytoskeleton | motor proteins | dynein | cell morphology | Drosophila

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Kinesin‐5 in Drosophila embryo mitosis: Sliding filament or spindle matrix mechanism?

Cited by 21 publications

References 55 publications

Depletion of kinesin-12, a myosin-IIB-interacting protein, promotes migration of cortical astrocytes

Depletion of kinesin-12, a myosin-IIB-interacting protein, promotes migration of cortical astrocytes

The Mechanical Properties of Early Drosophila Embryos Measured by High-Speed Video Microrheology

Kinesin-1 heavy chain mediates microtubule sliding to drive changes in cell shape

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