Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p

Wagner, Wolfgang

doi:10.1093/emboj/cdf650

Cited by 63 publications

(128 citation statements)

References 54 publications

(104 reference statements)

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“…To determine whether or not Shs1 exerts a distinct function from other septins in septin ring assembly and/or cytokinesis, we constructed shs1D cells in the W303 background. Proper disruption of SHS1 was verified by PCR (data not Wagner et al (2002) shown). The shs1D cells grew slowly at 25°and did not grow at 20° (Figure 1A).…”

Section: Resultsmentioning

confidence: 98%

Shs1 Plays Separable Roles in Septin Organization and Cytokinesis in Saccharomyces cerevisiae

Iwase

Luo

et al. 2007

Genetics

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In Saccharomyces cerevisiae, five septins (Cdc3, Cdc10, Cdc11, Cdc12, and Shs1/Sep7) form the septin ring at the bud neck during vegetative growth. We show here that disruption of SHS1 caused cold-sensitive growth in the W303 background, with cells arrested in chains, indicative of a cytokinesis defect. Surprisingly, the other four septins appeared to form an apparently normal septin ring in shs1D cells grown under the restrictive condition. We found that Myo1 and Iqg1, two components of the actomyosin contractile ring, and Cyk3, a component of the septum formation, were either delocalized or mislocalized in shs1D cells, suggesting that Shs1 plays supportive roles in cytokinesis. We also found that deletion of SHS1 enhanced or suppressed the septin defect in cdc10D and cdc11D cells, respectively, suggesting that Shs1 is involved in septin organization, exerting different effects on septin-ring assembly, depending on the composition of the septin subunits. Furthermore, we constructed an shs1-100c allele that lacks the coding sequence for the C-terminal 32 amino acids. This allele still displayed the genetic interactions with the septin mutants, but did not show cytokinesis defects as described above, suggesting that the roles of Shs1 in septin organization and cytokinesis are separable.

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Section: Resultsmentioning

confidence: 98%

Shs1 Plays Separable Roles in Septin Organization and Cytokinesis in Saccharomyces cerevisiae

Iwase

Luo

et al. 2007

Genetics

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“…Required for Myo1 targeting to the division site during cytokinesis, required for Iqg1 localization to the division site, and thus required for AMR assembly [Stevens and Davis, 1998;Boyne et al, 2000;Shannon and Li, 2000;Wagner et al, 2002;Luo et al, 2004;Fang et al, 2010] …”

Section: Mlc1mentioning

confidence: 99%

“…Catalytic subunit of chitin synthase III Required for the synthesis of chitin in the ''bud scar'' and the cell wall and may also play a role in SS formation [Shaw et al, 1991;Chuang and Schekman, 1996 [Kovacech et al, 1996] Chs1 Chitin synthase I Involved in septum repair at low pH after cell separation [Cabib et al, 1989;Cabib et al, 1992] Coordination of actomyosin ring and primary septum formation Septins GTP-binding and filament-forming proteins Required for AMR assembly and PS formation [Hartwell, 1971;Longtine et al, 1996 (p 297);Mino et al, 1998;Takizawa et al, 2000;Roh et al, 2002;Dobbelaere and Barral, 2004] Mlc1 ELC Required for AMR assembly and PS formation [Stevens and Davis, 1998;Boyne et al, 2000;Shannon and Li, 2000;Wagner et al, 2002;Luo et al, 2004;Fang et al, 2010] Iqg1 IQGAP Required for AMR assembly and PS formation [Epp and Chant, 1997;Shannon and Li, 1999;Boyne et al, 2000;Korinek et al, 2000;Ko et al, 2007;Tully et al, 2009;Fang et al, 2010] (Continued) n 720…”

Section: Chs3mentioning

confidence: 99%

Mechanisms of cytokinesis in budding yeast

Wloka

2012

Cytoskeleton

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Cytokinesis is essential for cell proliferation in all domains of life. Because the core components and mechanisms of cytokinesis are conserved from fungi to humans, the budding yeast Saccharomyces cerevisiae has served as an attractive model for studying this fundamental process. Cytokinesis in budding yeast is driven by two interdependent cellular events: actomyosin ring (AMR) constriction and the formation of a chitinous cell wall structure called the primary septum (PS), the functional equivalent of extracellular matrix remodeling during animal cytokinesis. AMR constriction is thought to drive efficient plasma membrane ingression as well as to guide PS formation, whereas PS formation is thought to stabilize the AMR during its constriction. Following the completion of the PS formation, two secondary septa (SS), consisting of glucans and mannoproteins, are synthesized at both sides of the PS. Degradation of the PS and a part of the SS by a chitinase and glucanases then enables cell separation. In this review, we discuss the mechanics of cytokinesis in budding yeast, highlighting its common and unique features as well as the emerging questions. © 2012 Wiley Periodicals, Inc.

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“…We hypothesized that the association of Myo2p with the accumulated post-Golgi vesicles in some late sec mutants (Wagner et al, 2002) might interfere with the localization of the myosin in these cells. To avoid this, we also examined cable and Myo2p distribution in yeast bearing conditional blocks in earlier steps of the secretory pathway.…”

Section: Polarized Secretion Maintains Cable Assembly Activity At Thementioning

confidence: 99%

“…However, this interpretation is complicated in that for many of these sec mutants, the overall localization of Myo2p was very poor, yet Myo2p itself is required to maintain cable assembly activity at the bud cortex. Thus, it was possible that in these mutants, the loss of bud cortex-associated cables was an indirect effect of delocalizing Myo2p.We hypothesized that the association of Myo2p with the accumulated post-Golgi vesicles in some late sec mutants (Wagner et al, 2002) might interfere with the localization of the myosin in these cells. To avoid this, we also examined cable and Myo2p distribution in yeast bearing conditional blocks in earlier steps of the secretory pathway.…”

mentioning

confidence: 99%

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

Pruyne

Gao

et al. 2004

MBoC

151

208

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Bud growth in yeast is guided by myosin-driven delivery of secretory vesicles from the mother cell to the bud. We find transport occurs along two sets of actin cables assembled by two formin isoforms. The Bnr1p formin assembles cables that radiate from the bud neck into the mother, providing a stable mother-bud axis. These cables also depend on septins at the neck and are required for efficient transport from the mother to the bud. The Bni1p formin assembles cables that line the bud cortex and target vesicles to varying locations in the bud. Loss of these cables results in morphological defects as vesicles accumulate at the neck. Assembly of these cables depends on continued polarized secretion, suggesting vesicular transport provides a positive feedback signal for Bni1p activation, possibly by rho-proteins. By coupling different formin isoforms to unique cortical landmarks, yeast uses common cytoskeletal elements to maintain stable and dynamic axes in the same cell. INTRODUCTIONProper cell polarization requires a balance between dynamism and stability. Persistent systems, such as the apical and basolateral domains of epithelial cells, show a higher stability than flexible systems, such as cells undergoing chemotaxis. However, both types can use similar cytoskeletal components, so an important task in understanding the control of polarity is to identify features that influence persistence, and how those features integrate with the core cytoskeletal machinery providing the physical expression of polarity.The process of bud growth of the yeast Saccharomyces cerevisiae provides a model for examining the control of polarity (for reviews, see Bretscher, 2003;Chang and Peter, 2003). Secretory organelles, such as the Golgi and endoplasmic reticulum, are distributed throughout the bud and mother cell, whereas post-Golgi secretory vesicles concentrate at discrete growth sites at the cell cortex. These vesicles are guided to these sites along what are essentially two axes of polarity: a stable axis directing traffic from the mother into the bud, and a dynamic axis that fine-tunes delivery from the bud neck to specific regions in the bud, sending vesicles first to the small bud tip, then to the entire bud surface, and finally back toward the neck during mother/daughter separation. On delivery to these locations, post-Golgi vesicles fuse with the cell surface to promote localized cell expansion.Two class-V myosins, with heavy chains encoded by MYO2 (Johnston et al., 1991) and MYO4 (Haarer et al., 1994), propel cellular components, including vesicles, organelles, mRNAs, and microtubules, from the mother into the bud during growth and organelle segregation. The myosins move along cables of actin filaments that radiate throughout the cell in arrays oriented toward growth sites (Adams and Pringle, 1984;Kilmartin and Adams, 1984).Assembly of these cables depends on two formin homologues, Bni1p and Bnr1p (Evangelista et al., 2002;Sagot et al., 2002a), members of a family of cytoskeletal regulatory proteins defined by conserved fo...

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Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p

Cited by 63 publications

References 54 publications

Shs1 Plays Separable Roles in Septin Organization and Cytokinesis in Saccharomyces cerevisiae

Shs1 Plays Separable Roles in Septin Organization and Cytokinesis in Saccharomyces cerevisiae

Mechanisms of cytokinesis in budding yeast

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

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