The novel proteins Rng8 and Rng9 regulate the myosin-V Myo51 during fission yeast cytokinesis

Wang, Ning; Presti, Libera Lo; Zhu, Yihua; Kang, Minhee; Wu, Zhengrong; Martin, Sophie G.; Wu, Jian-Qiu

doi:10.1083/jcb.201308146

Cited by 43 publications

(84 citation statements)

References 106 publications

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“…Nevertheless, Δ myo51 cells completed the coalescence of their nodes ~6 min later than wild-type cells (Figure 2E, Table 1). The Δ myo51 cells had no obvious morphological defects at room temperature and 22% of these cells were in cytokinesis similar to wildtype cells (Table 1) [23, 30]. Thus Myo51 makes a modest contribution to node coalescence.…”

Section: Resultsmentioning

confidence: 99%

“…Myo51 localized along For3p-dependent actin cables during interphase [23] giving a filamentous appearance in the cytoplasm (Figure 1A arrow). Beginning at time zero Myo51p concentrated in a narrow equatorial band and in filamentous structures between nodes [30] around the middle of the cell (Figures 1A asterisk and 1B), both dependent on actin filaments [23]. Myp2 began to accumulate in fully formed contractile rings at time +20 min (Figures 1A asterisk and 1B) [25].…”

Section: Resultsmentioning

confidence: 99%

“…Constriction subsequently reduced the circumferences of these large rings suggesting that they were not taut when newly assembled. The Δ myp2 Δmyo51 cells had cytokinetic defects including multiple septa and branched morphology (Figure S1B) [30]. …”

Section: Resultsmentioning

confidence: 99%

“…Cells treated with Latrunculin A to depolymerize actin filaments did not accumulate these spots of Myp2 even though the localization of mEGFP-Myo2p to nodes was unaffected (Figure 3G). Thus localization of both Myo51 [30] and Myp2 to the equator requires actin filaments.…”

Section: Resultsmentioning

confidence: 99%

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Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring

et al. 2015

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Summary Cytokinesis in fission yeast cells depends on conventional myosin-II (Myo2) to assemble and constrict a contractile ring of actin filaments. Less is known about the functions of an unconventional myosin-II (Myp2) and a myosin-V (Myo51) that are also present in the contractile ring. Myo2 appears in cytokinetic nodes around the equator 10 min before spindle pole body separation (cell cycle time −10 min) independent of actin filaments, followed by Myo51 at time zero and Myp2 at time +20 min, both located between nodes and dependent on actin filaments. We investigated the contributions of these three myosins to cytokinesis using a severely disabled mutation of the essential myosin-II heavy chain gene (myo2-E1) and deletion mutations of the other myosin heavy chain genes. Cells with only Myo2 assemble contractile rings normally. Cells with either Myp2 or Myo51 alone can assemble nodes and actin filaments into contractile rings, but complete assembly later than normal. Both Myp2 and Myo2 contribute to constriction of fully assembled rings at rates 55% of normal in cells relying on Myp2 alone and 25% of normal in cells with Myo2 alone. Myo51 alone cannot constrict rings but increases the constriction rate by Myo2 in Δmyp2 cells or Myp2 in myo2-E1 cells. Three myosins function in a hierarchal, complementary manner to accomplish cytokinesis with Myo2 and Myo51 taking the lead during contractile ring assembly and Myp2 making the greatest contribution to constriction.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring

et al. 2015

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“…Plan-Apo objective lens (Nikon) was used. Images were taken with the Volocity software package (Perkin-Elmer) and analyzed with ImageJ software (National Institutes of Health) as described (Wang et al 2014). Images in figures were maximum-intensity projections of z-sections spaced at 0.25 mm except where otherwise noted.…”

mentioning

confidence: 99%

The Activity-Dependent Regulation of Protein Kinase Stability by the Localization to P-Bodies

Zhang¹,

Shi²,

Varia³

et al. 2016

Genetics

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The eukaryotic cytoplasm contains a variety of ribonucleoprotein (RNP) granules in addition to the better-understood membrane-bound organelles. These granules form in response to specific stress conditions and contain a number of signaling molecules important for the control of cell growth and survival. However, relatively little is known about the mechanisms responsible for, and the ultimate consequences of, this protein localization. Here, we show that the Hrr25/CK1d protein kinase is recruited to cytoplasmic processing bodies (P-bodies) in an evolutionarily conserved manner. This recruitment requires Hrr25 kinase activity and the Dcp2 decapping enzyme, a core constituent of these RNP granules. Interestingly, the data indicate that this localization sequesters active Hrr25 away from the remainder of the cytoplasm and thereby shields this enzyme from the degradation machinery during these periods of stress. Altogether, this work illustrates how the presence within an RNP granule can alter the ultimate fate of the localized protein.KEYWORDS ribonucleoprotein granules; processing bodies; protein kinase; protein stability; Dcp2 decapping enzyme; casein kinase 1 T HE eukaryotic cell is subdivided into distinct functional areas by the presence of a variety of organelles. The best understood of these are the membrane-bound structures, like the nucleus, endoplasmic reticulum, and mitochondria. These traditional compartments are relatively stable and essential for the proper compartmentalization of the different reactions occurring in the cytoplasm. However, the cell also contains a collection of nonmembraneous organelles that are more dynamic in nature and form in response to particular cellular and environmental stimuli. Perhaps the two best characterized of these are the centrosome and nucleolus, which act as a microtubule-organizing center and a subnuclear site of ribosome assembly, respectively (Greenan et al. 2010;Brangwynne 2011;Brangwynne et al. 2011). This latter class also includes a number of recently identified cytoplasmic ribonucleoprotein (RNP) granules like the processing body (P-body) and stress granule (Anderson and Kedersha 2009;Balagopal and Parker 2009;Thomas et al. 2011). These cytoplasmic structures have been conserved through evolution and have been linked to a variety of human diseases, including certain neurodegenerative disorders, cancers, and autoimmune conditions (Li et al. 2013;Anderson et al. 2015). Despite this importance to human health, relatively little is known about the manner in which these RNP granules influence biological processes in the cell.These cytoplasmic RNP granules typically assemble in response to environmental stress or particular developmental cues (Thomas et al. 2011). Granule formation occurs as a consequence of the regulated coalescence of specific sets of proteins and translationally repressed mRNAs at discrete sites in the cytoplasm (Anderson and Kedersha 2009;Balagopal and Parker 2009). The presence of these core proteins often depends upon specific RNA-...

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Sliding filament and fixed filament mechanisms contribute to ring tension in the cytokinetic contractile ring

2019

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A fundamental challenge in cell biology is to understand how cells generate actomyosin‐based contractile force. Here we study the actomyosin contractile ring that divides cells during cytokinesis and generates tension by a mechanism that remains poorly understood. Long ago a muscle‐like sliding filament mechanism was proposed, but evidence for sarcomeric organization in contractile rings is lacking. We develop a coarse‐grained model of the fission yeast cytokinetic ring, incorporating the two myosin‐II isoforms Myo2 and Myp2 and severely constrained by experimental data. The model predicts that ring tension is indeed generated by a sliding filament mechanism, but a spatially and temporally homogeneous version of that in muscle. In this mechanism all pairs of oppositely oriented actin filaments are rendered tense as they are pulled toward one another and slide through clusters of myosin‐II. The mechanism relies on anchoring of actin filament barbed ends to the plasma membrane, which resists lateral motion and enables filaments to become tense when pulled by myosin‐II. A second fixed filament component is independent of lateral anchoring, generated by chains of like‐oriented actin filaments. Myo2 contributes to both components, while Myp2 contributes to the sliding filament component only. In the face of instabilities inherent to actomyosin contractility, organizational homeostasis is maintained by rapid turnover of Myo2 and Myp2, and by drag forces that resist lateral motion of actin, Myo2 and Myp2. Thus, sliding and fixed filament mechanisms contribute to tension in the disordered contractile ring without the need for the sarcomeric architecture of muscle.

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The novel proteins Rng8 and Rng9 regulate the myosin-V Myo51 during fission yeast cytokinesis

Abstract: In fission yeast, Rng8 and Rng9 form oligomers and cluster multiple Myo51 dimers to regulate Myo51 localization and function during cytokinesis.

Cited by 43 publications

References 106 publications

Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring

Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring

The Activity-Dependent Regulation of Protein Kinase Stability by the Localization to P-Bodies

Sliding filament and fixed filament mechanisms contribute to ring tension in the cytokinetic contractile ring

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