The Drosophila kinesin-like protein KLP3A is a midbody component required for central spindle assembly and initiation of cytokinesis.

Williams, Byron; Riedy, Michael F.; Williams, Erika V.; Gatti, Maurizio; Goldberg, Michael L.

doi:10.1083/jcb.129.3.709

Cited by 164 publications

(162 citation statements)

References 60 publications

(73 reference statements)

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“…During male meiosis, Drosophila KLP3A is only transiently associated with chromatin in early prophase, becomes excluded from chromatin during late prophase, and is dispersed in the cytoplasm from metaphase to anaphase (68). At the transition from anaphase to telophase, a fraction of XKLP1 and chromokinesin and essentially all of KLP3A become localized to the developing midbody (67)(68)(69).…”

Section: Potential Mitotic and Meiotic Motorsmentioning

confidence: 99%

Going mobile: microtubule motors and chromosome segregation.

Barton

Goldstein²

1996

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

156

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Proper chromosome segregation in eukaryotes depends upon the mitotic and meiotic spindles, which assemble at the time of cell division and then disassemble upon its completion. These spindles are composed in large part of microtubules, which either generate force by controlled polymerization and depolymerization or transduce force generated by molecular microtubule motors. In this review, we discuss recent insights into chromosome segregation mechanisms gained from the analyses of force generation during meiosis and mitosis. These analyses have demonstrated that members of the kinesin superfamily and

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Section: Potential Mitotic and Meiotic Motorsmentioning

confidence: 99%

Going mobile: microtubule motors and chromosome segregation.

Barton

Goldstein²

1996

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

156

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“…Kinesin-dependent movement of myosin II could also be independent of membranes. Interestingly, Drosophila cells expressing mutated KLP3A, a kinesin-like protein, fail to form a contractile ring during meiosis, whereas anaphase is not affected (27). Actin is not localized to the cleavage furrow region in these cells (28).…”

Section: Fig 2 Gfp-rlcmentioning

confidence: 99%

Myosin II localization during cytokinesis occurs by a mechanism that does not require its motor domain

Zang

Spudich

1998

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

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Myosin II generates force for the division of eukaryotic cells. The molecular basis of the spatial and temporal localization of myosin II to the cleavage furrow is unknown, although models often imply that interaction between myosin II and actin filaments is essential. We examined the localization of a chimeric protein that consists of the green f luorescent protein fused to the N terminus of truncated myosin II heavy chain in Dictyostelium cells. This chimera is missing the myosin II motor domain, and it does not bind actin filaments. Surprisingly, it still localizes to the cleavage furrow region during cytokinesis. These results indicate that myosin II localization during cytokinesis occurs through a mechanism that does not require it to be the force-generating element or to interact with actin filaments directly.

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“…Proteins outside the MAP65 family that are involved in stabilization of the phragmoplast or the central spindle have been identified in plants and animals (Williams et al 1995;Whittington et al 2001;Mishima et al 2002;Twell et al 2002). In addition, mammalian PRC1 interacts separately with many proteins that are involved in the formation of the midzone of the central spindle (Ban et al 2004;Kurasawa et al 2004;Zhu and Jiang 2005), suggesting that regulation of the dynamics of MT-containing structures must be very complex.…”

Section: Mapk Might Accelerate Expansion Of the Phragmoplast Via Phosmentioning

confidence: 99%

Phosphorylation of NtMAP65-1 by a MAP kinase down-regulates its activity of microtubule bundling and stimulates progression of cytokinesis of tobacco cells

Sasabe¹,

Soyano²,

Takahashi³

et al. 2006

Genes Dev.

169

177

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The tobacco mitogen-activated protein kinase (MAPK) cascade, which includes MAPK NRK1/NTF6, positively regulates expansion of the cytokinetic machinery known as the phragmoplast, which is followed by the synthesis of cell plates for completion of cell division. However, molecular events lying between the MAPK and phragmoplast expansion were not known. Here, we show that NRK1/NTF6 phosphorylates the threonine residue at position 579 in NtMAP65-1a, a microtubule-associated (MT-associated) protein. Levels of phosphorylated NtMAP65-1 increase during late M phase of the cell cycle, when NRK1/NTF6 is activated. Phosphorylated NtMAP65-1 is concentrated at the equator of phragmoplast, as is NRK1/NTF6. Overexpression of mutant forms of NtMAP65-1a that cannot be phosphorylated by NRK1 delays progression of the M phase and phragmoplast expansion, also rendering phragmoplast structures resistant to an MT-depolymerizing drug. Phosphorylation of NtMAP65-1 by NRK1/NTF6 down-regulates its MT-bundling activity in vitro. These results suggest that phosphorylation of NtMAP65-1 by NRK1/NTF6 also reduces its MT-bundling activity in vivo, which enhances destabilization and turnover of MTs at the phragmoplast equator, perhaps facilitating phragmoplast expansion.[Keywords: MAP65/PRC1; MAPK; cytokinesis; microtubule; microtubule-associated proteins; phragmoplast] Supplemental material is available at http://www.genesdev.org. Cell division in eukaryotes requires dynamic changes in cytoskeletal structures that consist of microtubules (MTs) and microfilaments Jürgens 2005). During cytokinesis, the final critical step in the cell division, cells form a cytokinesis-specific apparatus (known as the central spindle in animals and the phragmoplast in plants) that plays a key role in cytokinesis (Field et al. 1999;. These structures develop from late anaphase to telophase between the two daughter nuclei, and consist of two bundles of antiparallel MTs. As cytokinesis proceeds, the central spindle becomes compacted in animal cells and the phragmoplast expands centrifugally in plant cells, and new membranes and/or cell walls are generated inside or outside the midzone of the central spindle or the phragmoplast to separate the two daughter cells from each other (Otegui et al. 2005). These dynamic processes appear to be mediated by the turnover of MTs, which involves the depolymerization of MTs and the polymerization of tubulin at the plus ends (Shelden and Wadsworth 1990;Asada et al. 1991;Hush et al. 1994;Straight and Field 2000). Recently, Austin et al. (2005) have reported that somatic-type phragmoplast MTs do not interdigitate at the cell plate mid-line and that distinct MT plus-end geometries are seen during the different stages of cytokinesis.The members of the MAP65/Ase1/PRC1 family (designated the MAP65 family herein)-including plant MAP65, yeast Ase1, and human PRC1-participate in the bundling of MTs (Chang-Jie and Sonobe 1993;Chan et al. 1999;Mollinari et al. 2002;Schuyler et al. 2003;

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The Drosophila kinesin-like protein KLP3A is a midbody component required for central spindle assembly and initiation of cytokinesis.

Cited by 164 publications

References 60 publications

Going mobile: microtubule motors and chromosome segregation.

Going mobile: microtubule motors and chromosome segregation.

Myosin II localization during cytokinesis occurs by a mechanism that does not require its motor domain

Phosphorylation of NtMAP65-1 by a MAP kinase down-regulates its activity of microtubule bundling and stimulates progression of cytokinesis of tobacco cells

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