The Msd1–Wdr8–Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies

Yukawa, Masashi; Ikebe, Chiho; Toda, Takashi

doi:10.1083/jcb.201412111

Cited by 57 publications

(116 citation statements)

References 84 publications

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“…Interestingly, orthologues of SSX2IP and WDR8 have been found in conserved complexes not only in human cells, as shown here, but previously in Aspergillus nidulans (Shen and Osmani, 2013), in Schizosaccharomyces pombe (Toya et al, 2007;Yukawa et al, 2015) and X. laevis (O.G., unpublished observation). This indicates that the SSX2IP-WDR8 protein module must be highly conserved throughout eukaryotic evolution.…”

Section: Discussionmentioning

confidence: 58%

“…Here, we have identified human WDR8 (also known as WRAP73) as an interacting partner of the satellite components SSX2IP and PCM1 (Shen and Osmani, 2013;Yukawa et al, 2015). We show that, in contrast to SSX2IP and PCM1, which only associate with cytoplasmic satellite complexes, a large fraction of WDR8 localises to centrioles and basal bodies even when satellites are dispersed.…”

Section: Introductionmentioning

confidence: 97%

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WDR8 is a centriolar satellite and centriole-associated protein that promotes ciliary vesicle docking during ciliogenesis

Kurtulmus

Wang

Ruppert

et al. 2016

Journal of Cell Science

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Ciliogenesis initiates at the mother centriole through a series of events that include membrane docking, displacement of cilia-inhibitory proteins and axoneme elongation. Centriolar proteins, in particular at distal and subdistal appendages, carry out these functions. Recently, cytoplasmic complexes named centriolar satellites have also been shown to promote ciliogenesis. Little is known about the functional and molecular relationship between appendage proteins, satellites and cilia biogenesis. Here, we identified the WD-repeat protein 8 (WDR8, also known as WRAP73) as a satellite and centriolar component. We show that WDR8 interacts with the satellite proteins SSX2IP and PCM1 as well as the centriolar proximal end component Cep135. Cep135 is required for the recruitment of WDR8 to centrioles. Depletion experiments revealed that WDR8 and Cep135 have strongly overlapping functions in ciliogenesis. Both are indispensable for ciliary vesicle docking to the mother centriole and for unlocking the distal end of the mother centriole from the ciliary inhibitory complex CP110-Cep97. Our data thus point to an important function of centriolar proximal end proteins in ciliary membrane biogenesis, and establish WDR8 and Cep135 as two factors that are essential for the initial steps of ciliation.

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Section: Discussionmentioning

confidence: 58%

Section: Introductionmentioning

confidence: 97%

WDR8 is a centriolar satellite and centriole-associated protein that promotes ciliary vesicle docking during ciliogenesis

Kurtulmus

Wang

Ruppert

et al. 2016

Journal of Cell Science

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“…For example, it has been reported that overexpression of Ned1 (11) (a protein known to influence the stability of chromosome) or Mia1 (12), deletion of Msd1 (13), or malfunction of the Msd1-Wdr8-Pkl1 complex (14) and the knockout of pkl1 (15), all induce improper anchoring of MTs to the SPBs, resulting in panhandle-shaped protrusions of NE driven by elongating microtubule bundles. Similar effect can also be achieved by the abscission of SPBs using laser microsurgery (16,17).…”

Section: Introductionmentioning

confidence: 99%

Shape Transformation of the Nuclear Envelope during Closed Mitosis

Zhu

Zheng

Liu

et al. 2016

Biophysical Journal

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The nuclear envelope (NE) in lower eukaryotes such as Schizosaccharomyces pombe undergoes large morphology changes during closed mitosis. However, which physical parameters are important in governing the shape evolution of the NE, and how defects in the dividing chromosomes/microtubules are reflected in those parameters, are fundamental questions that remain unresolved. In this study, we show that improper separation of chromosomes in genetically deficient cells leads to membrane tethering or asymmetric division in contrast to the formation of two equal-sized daughter nuclei in wild-type cells. We hypothesize that the poleward force is transmitted to the nuclear membrane through its physical contact with the separated sister chromatids at the two spindle poles. A theoretical model is developed to predict the morphology evolution of the NE where key factors such as the work done by the poleward force and bending and surface energies stored in the membrane have been taken into account. Interestingly, the predicted phase diagram, summarizing the dependence of nuclear shape on the size of the load transmission regions, and the pole-to-pole distance versus surface area relationship all quantitatively agree well with our experimental observations, suggesting that this model captures the essential physics involved in closed mitosis.

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“…2D). In the mitotic spindle pole body, Pkl1 is required for the localization of Msd1 and the mitosis-specific spindle pole body component Wdr8; it cooperatively interacts with these two proteins to mediate the spindle anchoring, where it counteracts the outward pushing forces that are generated by Cut7 (Yukawa et al, 2015). In addition, Pkl1 also functions as the spindle assembly checkpoint, which regulates chromosome bi-orientation by mediating the spindle pole assembly (Grishchuk et al, 2007).…”

Section: Tug-of-war Between Kinesin-14 and Kinesin-5 In Spindle Assemblymentioning

confidence: 99%

“…First, kinesin-14 motors have the intrinsic ability to focus the minus-ends of microtubules into spindle poles, but kinesin-5 motors counteract focusing of the microtubule plus-ends at the poles (Hentrich and Surrey, 2010). Second, kinesin-14 motors generate inward pulling forces on spindles, whereas the kinesin-5 motors have been shown to generate outwards forces on spindles in vitro (Yukawa et al, 2015). Another mechanism by which kinesin-14 and kinesin-5 counterbalance their activities does not require the motor domains but is mediated primarily by the tail, i.e.…”

Section: Box 2 Microtubule End-binding Proteins and Plus-end Trackingmentioning

confidence: 99%

Molecular mechanisms of kinesin-14 motors in spindle assembly and chromosome segregation

She

Yang

2017

Journal of Cell Science

106

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During eukaryote cell division, molecular motors are crucial regulators of microtubule organization, spindle assembly, chromosome segregation and intracellular transport. The kinesin-14 motors are evolutionarily conserved minus-end-directed kinesin motors that occur in diverse organisms from simple yeasts to higher eukaryotes. Members of the kinesin-14 motor family can bind to, crosslink or slide microtubules and, thus, regulate microtubule organization and spindle assembly. In this Commentary, we present the common subthemes that have emerged from studies of the molecular kinetics and mechanics of kinesin-14 motors, particularly with regard to their non-processive movement, their ability to crosslink microtubules and interact with the minus-and plusends of microtubules, and with microtubule-organizing center proteins. In particular, counteracting forces between minus-enddirected kinesin-14 and plus-end-directed kinesin-5 motors have recently been implicated in the regulation of microtubule nucleation. We also discuss recent progress in our current understanding of the multiple and fundamental functions that kinesin-14 motors family members have in important aspects of cell division, including the spindle pole, spindle organization and chromosome segregation.

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The Msd1–Wdr8–Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies

Abstract: Msd1–Wdr8 are delivered by Pkl1 to mitotic spindle pole bodies, where the Msd1–Wdr8–Pkl1 complex anchors the minus ends of spindle microtubules and antagonizes the outward-pushing forces generated by Cut7/kinesin-5 in fission yeast.

Cited by 57 publications

References 84 publications

WDR8 is a centriolar satellite and centriole-associated protein that promotes ciliary vesicle docking during ciliogenesis

WDR8 is a centriolar satellite and centriole-associated protein that promotes ciliary vesicle docking during ciliogenesis

Shape Transformation of the Nuclear Envelope during Closed Mitosis

Molecular mechanisms of kinesin-14 motors in spindle assembly and chromosome segregation

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