Augmin shapes the anaphase spindle for efficient cytokinetic furrow ingression and abscission

Uehara, Ritei; Kamasaki, Tomoko; Hiruma, Shota; Poser, Ina; Yoda, Kinya; Yajima, Junichiro; Gerlich, Daniel W.; Goshima, Gohta

doi:10.1091/mbc.e15-02-0101

Cited by 24 publications

(33 citation statements)

References 82 publications

(125 reference statements)

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“…Rat anti‐α‐tubulin (YOL1/34, EMD Millipore, Temecula, CA; 1 : 500 for IB), rat anti‐GFP (GF090R, Nacalai, Kyoto, Japan; 1: 1000 for IB), goat antianillin (sc‐54859, Santa Cruz Biotechnology, Dallas, TX; 1 : 500 for IF), rabbit antianillin (A301‐405A, Bethyl Laboratories, Montgomery, TX; 1 : 50 for IB), mouse antiezrin (sc‐58758, Santa Cruz Biotechnology; 1 : 100 for IF and 1 : 100 for IB), rabbit antiradixin (EP1862Y, GeneTex, Irvine, CA; 1 : 200 for IF and 1 : 10 000 for IB), rabbit antimoesin (3150, Cell Signaling Technology, Danvers, MA; 1 : 300 for IF and 1 : 1000 for IB), rabbit antisupervillin (NBP1‐90363, Novus Biotechnologicals, Littleton, CO; 1 : 200 for IF and 1 : 500 for IB), mouse anti‐RhoA (sc‐418, Santa Cruz Biotechnology; 1 : 100 for IF), rabbit anti‐RhoA, B, C (EPR18299, Abcam Cambridge, United Kingdom; 1: 500 for IF), rabbit antimyosin IIA (a gift from Dr. K. Owaribe; 1 : 1000 for IF) , mouse anti‐MLKP1 (a gift from Dr. K. Yoda; 1 : 2 for IF) , and fluorescence‐ or horseradish peroxidase‐conjugated secondary antibodies (Jackson ImmunoResearch Laboratories, West Grove, PA; 1 : 1000 for IF and IB) were purchased from the suppliers and used at the dilutions as indicated.…”

Section: Methodsmentioning

confidence: 99%

Dynamics and function ofERMproteins during cytokinesis in human cells

et al. 2017

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The molecular mechanism that governs cytoskeleton-membrane interaction during animal cytokinesis remains elusive. Here, we investigated the dynamics and functions of ERM (Ezrin/Radixin/Moesin) proteins during cytokinesis in human cultured cells. We found that ezrin is recruited to the cleavage furrow through its membrane-associated domain in a cholesterol-dependent but largely Rho-independent manner. While ERMs are dispensable for furrow ingression, they play a pivotal role in contractile activity of the polar cortex. Notably, when anillin and supervillin are codepleted, ERMs increasingly accumulate at the cleavage furrow and substantially contribute to the furrow ingression. These results reveal a supportive role of ERMs in cortical activities during cytokinesis, and also provide insight into the selective mechanism that preferentially associates cytokinesis-relevant proteins with the division site.

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Section: Methodsmentioning

confidence: 99%

Dynamics and function ofERMproteins during cytokinesis in human cells

et al. 2017

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“…The bidirectional cortical flow towards the cell equator contributes to the equatorial accumulation of the actomyosin network and to the cleavage furrow formation (DeBiasio et al, 1996;Reymann et al, 2016;Salbreux et al, 2009;Turlier et al, 2014;Werner et al, 2007;Zhou and Wang, 2008). In addition to the central spindle, the molecules for equatorial simulation can be recruited to the anti-parallel overlaps of the equatorial astral microtubules (Argiros et al, 2012;D'Avino et al, 2006;Nguyen et al, 2014;Nishimura and Yonemura, 2006;Su et al, 2014;Uehara et al, 2016) and to the microtubule ends that laterally associate with the furrow cortex in monopolar cytokinesis (Canman et al, 2003;Hu et al, 2008;Kitagawa et al, 2013;Shrestha et al, 2012). It has also been reported that precise microtubule polymerization/depolymerization dynamics does not play a crucial role for furrow induction (Strickland et al, 2005).…”

Section: Materials and Methods Andmentioning

confidence: 99%

Polar relaxation by dynein-mediated removal of cortical myosin II

Chapa-y-Lazo

Hamanaka

Wray

et al. 2019

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Nearly 6 decades ago, Lewis Wolpert proposed the relaxation of the polar cell cortex by the radial arrays of astral microtubules as a mechanism for cleavage furrow induction (White and Borisy, 1983;Wolpert, 1960). While this mechanism has remained controversial (Rappaport, 1996), recent work has provided evidence for polar relaxation by astral microtubules (Chen et al., 2008; Dechant and Glotzer, 2003; Foe and Dassow, 2008;Murthy and Wadsworth, 2008;Werner et al., 2007), although its molecular mechanisms remain elusive. Here, using C. elegans embryos, we show that polar relaxation is achieved through dynein-mediated removal of myosin II from the polar cortexes. Mutants that position centrosomes closer to the polar cortex accelerated furrow induction whereas suppression of dynein activity delayed furrowing. We provide evidence that dynein-mediated removal of myosin II from the polar cortexes triggers cortical flow towards the cell equator, which induces the assembly of the actomyosin contractile ring. These studies for the first time provide a molecular basis for the aster-dependent polar relaxation, which works in parallel with equatorial stimulation to promote robust cytokinesis. Results and DiscussionDuring animal cell cytokinesis, cleavage by constriction of an actomyosin contractile ring is spatially coupled to chromosome segregation by the mitotic apparatus (D'Avino et al., 2015;Green et al., 2012). The best-understood mechanism for spatial coupling is chemical signaling via activation of Rho GTPase at the cell equator by the central spindle, which is mediated by centralspindlin, a microtubule-

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“…Previously, we had found that depletion of a spindle-associated protein complex, augmin, suppressed MT generation within the mitotic spindle and instead enhanced development of prominent astral MTs during anaphase in HeLa cells (Uehara et al, 2016). Therefore, we tested the effect of augmin depletion on the progression of centriole disengagement and subsequent centriole duplication in haploid HAP1 cells.…”

Section: Ploidy-dependent Difference In Astral Mt Development Determimentioning

confidence: 96%

Uncoordinated centrosome duplication cycle underlies the instability of non-diploid states in mammalian somatic cells

Yaguchi

Matsui

Yamamoto

et al. 2017

Preprint

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2 SummaryYaguchi et al. show that a delay or acceleration of centriole licensing compromises the control of centrosome number in haploid or tetraploid human cells, respectively, suggesting a cellular basis of the instability of non-diploid somatic cells in mammals. AbstractIn animals, somatic cells are usually diploid and are unstable when haploid for unknown reasons. In this study, by comparing isogenic human cell lines with different ploidies, we found frequent centrosome loss specifically in the haploid state, which profoundly contributed to haploid instability through monopolar spindle formation and subsequent mitotic defects. We also found that efficiency of centriole licensing and duplication, but not that of DNA replication, changes proportionally to ploidy level, causing gradual loss or frequent overduplication of centrioles in haploid and tetraploid cells, respectively. Centriole licensing efficiency seemed to be modulated by astral microtubules, whose development scaled with ploidy level, and artificial enhancement of aster formation in haploid cells restored centriole licensing efficiency to diploid levels. Haploid-specific centrosome loss was also observed in parthenogenetic mouse embryos. We propose that incompatibility between the centrosome duplication and DNA replication cycles arising from different scaling properties of these bioprocesses upon ploidy changes, underlies the instability of non-diploid somatic cells in mammals.

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Augmin shapes the anaphase spindle for efficient cytokinetic furrow ingression and abscission

Cited by 24 publications

References 82 publications

Dynamics and function ofERMproteins during cytokinesis in human cells

Dynamics and function ofERMproteins during cytokinesis in human cells

Polar relaxation by dynein-mediated removal of cortical myosin II

Uncoordinated centrosome duplication cycle underlies the instability of non-diploid states in mammalian somatic cells

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