Genetic suppression of defective profilin by attenuated Myosin II reveals a potential role for Myosin II in actin dynamics in vivo in fission yeast

Zambon, Paola; Palani, Saravanan; Jadhav, Shekhar Sanjay; Gayathri, P.; Balasubramanian, Mohan K.

doi:10.1091/mbc.e20-04-0224

Cited by 3 publications

(4 citation statements)

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“…The actin-binding proteins profilin (Cdc3) and tropomyosin (Cdc8) localize to the contractile ring and play essential roles in the formation, stabilization, and maintenance of actin filaments for the CAR during cytokinesis ( Balasubramanian et al, 1992 ; Balasubramanian et al, 1994 ). Cells expressing the hypomorphic cdc3-124 and cdc8-110 alleles are defective in CAR assembly and colony formation at 32°C and 34°C, respectively ( Figure 6A ; Balasubramanian et al, 1996 ; Zambon et al, 2020 ). Incubation of cdc3-124 and cdc8-110 cells during 4 hr at the restrictive temperature (34°C), prompted a reduction in total protein levels of a genomic For3-3GFP fusion as compared to wild type cells ( Figure 6B ).…”

Section: Resultsmentioning

confidence: 99%

“…Considering that the decrease in total For3 levels at high temperature is Sty1-dependent (Figure 5-figure supplement 3), these findings suggest that a SAPK-mediated mechanism enhances For3 in vivo ubiquitination and degradation in response to stress.The actin-binding proteins profilin (Cdc3) and tropomyosin (Cdc8) localize to the contractile ring and play essential roles in the formation, stabilization, and maintenance of actin filaments for the CAR during cytokinesis[51,52]. Cells expressing the hypomorphic cdc3-124 and cdc8-110 alleles are defective in CAR assembly and colony formation at 32 and 34ºC, respectively (Figure 6A)[53,54]. Incubation of cdc3-124 and cdc8-110 cells during 4 hours at the restrictive temperature (34ºC), prompted a reduction in total protein levels of a genomic For3-3GFP fusion as compared to wild type cells (Figure 6B).…”

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Stress-activated MAPK signaling controls fission yeast actomyosin ring integrity by modulating formin For3 levels

Gómez-Gil

Martín‐García

Vicente-Soler

et al. 2020

eLife

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Cytokinesis, which enables the physical separation of daughter cells once mitosis has been completed, is executed in fungal and animal cells by a contractile actin- and myosin-based ring (CAR). In the fission yeast Schizosaccharomyces pombe the formin For3 nucleates actin cables and also co-operates for CAR assembly during cytokinesis. Mitogen-Activated Protein Kinases (MAPKs) regulate essential adaptive responses in eukaryotic organisms to environmental changes. We show that the Stress Activated Protein Kinase pathway (SAPK) and its effector, MAPK Sty1, downregulates CAR assembly in S. pombe when its integrity becomes compromised during cytoskeletal damage and stress by reducing For3 levels. Accurate control of For3 levels by the SAPK pathway may thus represent a novel regulatory mechanism of cytokinesis outcome in response to environmental cues. Conversely, SAPK signalling favours CAR assembly and integrity in its close relative S. japonicus, revealing a remarkable evolutionary divergence of this response within the fission yeast clade.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Stress-activated MAPK signaling controls fission yeast actomyosin ring integrity by modulating formin For3 levels

Gómez-Gil

Martín‐García

Vicente-Soler

et al. 2020

eLife

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“…This is consistent with defective Arp2/3 complex based actin nucleation of R- β -actin which we observed previously ( Chin et al ., 2022). Thicker cables are an indicator of failed myosin function or an anti-correlation between patches and cables in fission yeast ( Balasubramanian et al ., 1996, 1998; Burke et al ., 2014; Zambon et al ., 2020). It is very likely based on our in vitro analysis that the charge differences in REE-actin and its consequent decrease in myosin II interaction led to the cytokinesis defects that we observed in the REE strain.…”

Section: Discussionmentioning

confidence: 99%

Structure and physiological investigation of arginylated actin

Pinto,

Bakker,

Suchenko

et al. 2024

Preprint

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Actin is an evolutionarily conserved cytoskeletal protein with crucial roles in cell polarity, division, migration, and muscle contraction. Actin function is regulated in part by posttranslational modifications. One such modification in non-muscle cells is arginylation, in which an arginine residue is added to the N-terminus of β-actin. What is the structure of arginylated β-actin (R-β-actin), are its interactions with other proteins altered and what phenotypes result when R-β-actin is the sole actin isoform present in the cell? Here we report the 4.2 Å structure of ADP-bound human R-β-actin filaments, the overall structure of which is nearly identical to the filaments made of non-arginylated actin.In vitrofunctional assays using isoform-pure actins with defined post-translational modifications reveal that the interaction between myosin-II and actin is altered upon actin arginylation, due to frequent detachment of myosin-II from R-actin filaments.In vivo, we find that replacement of the only actin gene inSchizosaccharomyces pombewith a synthetic gene encoding R-Sp-actin reduces Arp2/3-based actin patches while thickening the formin-induced actin. Furthermore, consistent with altered interactions between myosin-II and R-actin filaments, the assembly and constriction of cytokinetic actomyosin ring are perturbed in the R-Sp-actin cells. Thus, despite the overall structural similarity of arginylated and non-arginylated actin filaments, actin arginylation affects actin filament assortment into distinct subcellular structures and its interaction with myosin II.

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“…1a). As compared to wild-type cells, a hypomorphic mutant in the actin-binding protein profilin (cdc3-124), which plays essential roles in the formation, stabilization, and maintenance of actin filaments for the CAR during cytokinesis, is growth sensitive to very low LatA concentrations (Zambon et al 2020) (Fig. 1b).…”

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Negative control of cytokinesis by stress-activated MAPK signaling

2021

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Mitogen-activated protein kinase (MAPK) signalling pathways regulate multiple cellular functions in eukaryotic organisms in response to environmental cues, including the dynamic remodeling of the actin cytoskeleton. The fission yeast S. pombe is an optimal model to investigate the conserved regulatory mechanisms of cytokinesis, which relies in an actomyosin-based contractile ring (CAR) that prompts the physical separation of daughter cells during cellular division. Our group has recently shown that p38 MAPK ortholog Sty1, the core component of the stress-activated pathway (SAPK), negatively modulates CAR assembly and integrity in S. pombe during actin cytoskeletal damage induced with Latrunculin A and in response to environmental stress. This response involves downregulation of protein levels of the formin For3, which assembles actin filaments for cables and the CAR, likely through an ubiquitin-mediated degradation mechanism. Contrariwise, Sty1 function positively reinforces CAR assembly during stress in the close relative dimorphic fission yeast S. japonicus. The opposite effect of SAPK signaling on CAR integrity may represent an evolutionary refined adaptation to cope with the marked differences in cytokinesis onset in both fission yeast species.

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Genetic suppression of defective profilin by attenuated Myosin II reveals a potential role for Myosin II in actin dynamics in vivo in fission yeast

Cited by 3 publications

References 54 publications

Stress-activated MAPK signaling controls fission yeast actomyosin ring integrity by modulating formin For3 levels

Stress-activated MAPK signaling controls fission yeast actomyosin ring integrity by modulating formin For3 levels

Structure and physiological investigation of arginylated actin

Negative control of cytokinesis by stress-activated MAPK signaling

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