Nonmedially assembled F-actin cables incorporate into the actomyosin ring in fission yeast

Huang, Junqi; Huang, Yinyi; Yu, Haochen; Subramanian, Dhivya; Padmanabhan, Anup; Thadani, Rahul; Tao, Yaqiong; Tang, Xie; Wedlich‐Söldner, Roland; Balasubramanian, Mohan K.

doi:10.1083/jcb.201209044

Cited by 97 publications

(126 citation statements)

References 67 publications

Supporting

Mentioning

111

Contrasting

Unclassified

Order By: Relevance

“…Gef1-mNG persists on both sides of the septum barrier in 40% of cells treated with LatA, but not in mock DMSO-treated cells ( Figure 3C). Cells undergoing ring constriction and septum formation display actin cables as well as Arp2/3-complex-dependent patches at the division site (Coffman et al, 2013;Gachet and Hyams, 2005;Huang et al, 2012;Wang et al, 2016). LatA treatment removes all types of filamentous actin structures (Spector et al, 1983).…”

Section: Scd1 Promotes Gef1 Removal From the Division Site At The Endmentioning

confidence: 99%

A novel interplay between GEFs orchestrates Cdc42 activity during cell polarity and cytokinesis

Hercyk

Rich

Das

2018

Preprint

View full text Add to dashboard Cite

Cdc42, a conserved regulator of cell polarity, is activated by two GEFs, Gef1 and Scd1, in fission yeast. While gef1 and scd1 mutants exhibit distinct phenotypes, how they do so is unclear given that they activate the same GTPase. Using the GEF localization pattern during cytokinesis as a paradigm, we report a novel interplay between Gef1 and Scd1 that spatially modulates Cdc42. We find that Gef1 promotes Scd1 localization to the division site during cytokinesis and to the new end during polarized growth through the recruitment of the scaffold Scd2 via a Cdc42 feedforward pathway. Gef1-mediated Scd1 recruitment at the new end enables the transition from monopolar to bipolar growth. Reciprocally, Scd1 restricts Gef1 localization to prevent ectopic Cdc42 activation during cytokinesis to promote cell separation and during interphase to maintain cell shape. Our findings reveal an elegant regulatory pattern in which Gef1 establishes new sites of Scd1-mediated Cdc42 activity, while Scd1 restricts Gef1 to functional sites. We propose that crosstalk between GEFs is a conserved mechanism that orchestrates Cdc42 activation during complex cellular processes.Summary StatementCdc42 GEFs Gef1 and Scd1 crosstalk to fine-tune Cdc42 activity. This crosstalk promotes bipolar growth and maintains cell shape in fission yeast.

show abstract

Section: Scd1 Promotes Gef1 Removal From the Division Site At The Endmentioning

confidence: 99%

A novel interplay between GEFs orchestrates Cdc42 activity during cell polarity and cytokinesis

Hercyk

Rich

Das

2018

Preprint

View full text Add to dashboard Cite

show abstract

“…4D) in myo2 + strains. These results suggest that binding sites for Myo3 on the ring are available after the completed assembly of the ring, and diffused Myo3 molecules directly bind to the sites rather than migrating towards the ring through ring-associated actin tracks (Arai and Mabuchi, 2002;Huang et al, 2012).…”

Section: Accumulation Kinetics Of Mutant Myo3 Proteins During Cytokinmentioning

confidence: 99%

An actin–myosin-II interaction is involved in maintaining the contractile ring in fission yeast

Takaine

Numata

Nakano

2015

Journal of Cell Science

View full text Add to dashboard Cite

The actomyosin-based contractile ring, which assembles at the cell equator, maintains its circularity during cytokinesis in many eukaryotic cells, ensuring its efficient constriction. Although consistent maintenance of the ring is one of the mechanisms underpinning cytokinesis, it has not yet been fully addressed. We here investigated the roles of fission yeast myosin-II proteins [Myo2 and Myo3 (also known as Myp2)] in ring maintenance during cytokinesis, with a focus on Myo3. A sitedirected mutational analysis showed that the motor properties of Myo3 were involved in its accumulation in the contractile ring. The assembled ring was often deformed and not properly maintained under conditions in which the activities of myosin-II proteins localizing to the contractile ring were decreased, leading to inefficient cell division. Moreover, Myo3 appeared to form motile clusters on the ring. We propose that large assemblies of myosin-II proteins consolidate the contractile ring by continuously binding to F-actin in the ring, thereby contributing to its maintenance.

show abstract

“…This process has been modeled using physiological parameters that recapitulate observations in wildtype and mutant conditions. Some F-actin in the ring is recruited from filaments that assemble at peripheral sites of nucleation (Huang et al 2012). However, as discussed previously, other mechanisms might suffice for functional ring assembly in fission yeast.…”

Section: Contractile Ring Assembly In Fission Yeastmentioning

confidence: 89%

Cytokinesis in Metazoa and Fungi

Glotzer

2016

Cold Spring Harb Perspect Biol

View full text Add to dashboard Cite

SUMMARYCell division-cytokinesis-involves large-scale rearrangements of the entire cell. Primarily driven by cytoskeletal proteins, cytokinesis also depends on topological rearrangements of the plasma membrane, which are coordinated with nuclear division in both space and time. Despite the fundamental nature of the process, different types of eukaryotic cells show variations in both the structural mechanisms of cytokinesis and the regulatory controls. In animal cells and fungi, a contractile actomyosin-based structure plays a central, albeit flexible, role. Here, the underlying molecular mechanisms are summarized and integrated and common themes are highlighted.

show abstract

Nonmedially assembled F-actin cables incorporate into the actomyosin ring in fission yeast

Cited by 97 publications

References 67 publications

A novel interplay between GEFs orchestrates Cdc42 activity during cell polarity and cytokinesis

A novel interplay between GEFs orchestrates Cdc42 activity during cell polarity and cytokinesis

An actin–myosin-II interaction is involved in maintaining the contractile ring in fission yeast

Cytokinesis in Metazoa and Fungi

Contact Info

Product

Resources

About