Localization of Type I Myosin and F-actin to the Leading Edge Region of the Forespore Membrane in Schizosaccharomyces pombe

Itadani, Akiko; Nakamura, Taro; Shimoda, Chikashi

doi:10.1247/csf.06027

Cited by 22 publications

(32 citation statements)

References 41 publications

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“…By electron microscopy, the leading edge of FSM is observed as an electron dense structure, which is apparently distinct from the FSM (Hirata, unpublished data). Several proteins have been identified as leading edge components both in S. cerevisiae and S. pombe (Knop and Strasser, 2000;MorenoBorchart et al, 2001;Nickas and Neiman, 2002;Okuzaki et al, 2003;Itadani et al, 2006). In S. pombe, Meu14 is one of the leading edge components.…”

Section: Closure Of the Fsmmentioning

confidence: 99%

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Live Observation of Forespore Membrane Formation in Fission Yeast

Nakamura

Asakawa

Nakase

et al. 2008

MBoC

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Sporulation in the fission yeast Schizosaccharomyces pombe is a unique biological process in that the plasma membrane of daughter cells is assembled de novo within the mother cell cytoplasm. A double unit membrane called the forespore membrane (FSM) is constructed dynamically during meiosis. To obtain a dynamic view of FSM formation, we visualized FSM in living cells by using green fluorescent protein fused with Psy1, an FSM-resident protein, together with the nucleus or microtubules. The assembly of FSM initiates in prophase II, and four FSMs in a cell expand in a synchronous manner at the same rate throughout meiosis II. After the meiosis II completes, FSMs continue to expand until closure to form the prespore, a spore precursor. Prespores are initially ellipsoidal, and eventually become spheres. FSM formation was also observed in the sporulation-deficient mutants spo3, spo14, and spo15. In the spo15 mutant, the initiation of FSM formation was completely blocked. In the spo3 mutant, the FSM expanded normally during early meiosis II, but it was severely inhibited during late and postmeiosis, whereas in the spo14 mutant, membrane expansion was more severely inhibited throughout meiosis II. These observations suggest that FSM expansion is composed of two steps, early meiotic FSM expansion and late and post meiotic FSM expansion. Possible regulatory mechanisms of FSM formation in fission yeast are discussed.

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Section: Closure Of the Fsmmentioning

confidence: 99%

“…Prespores might become spherical concomitantly with formation of the spore wall. Alternatively, at this stage, actin patches are dispersed at the periphery of the prespores (Petersen et al, 1998;Itadani et al, 2006;Ohtaka et al, 2007). Actin relocalization may be required for spherical shaping of spores.…”

Section: Spore Morphogenesismentioning

confidence: 99%

Live Observation of Forespore Membrane Formation in Fission Yeast

Nakamura

Asakawa

Nakase

et al. 2008

MBoC

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“…Cam2p functions in mating and meiosis, and is essential for sporulation at elevated temperatures (Itadani et al, 2006), but its role in vegetative growth and in the function of Myo1p is not understood. Cam2p shares its closest amino acid sequence homology with calmodulin (41% identity) and the ELC Cdc4p (35%).…”

Section: Introductionmentioning

confidence: 99%

A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase

Sammons

James

Clayton

et al. 2011

Journal of Cell Science

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SummaryFission yeast myosin-I (Myo1p) not only associates with calmodulin, but also employs a second light chain called Cam2p. cam2 cells exhibit defects in cell polarity and growth consistent with a loss of Myo1p function. Loss of Cam2p leads to a reduction in Myo1p levels at endocytic patches and a 50% drop in the rates of Myo1p-driven actin filament motility. Thus, Cam2p plays a significant role in Myo1p function. However, further studies indicated the existence of an additional Cam2p-binding partner. Cam2p was still present at cortical patches in myo1 cells (or in myo1-IQ2 mutants, which lack an intact Cam2p-binding motif), whereas a cam2 null (cam2) suppressed cytokinesis defects of an essential light chain (ELC) mutant known to be impaired in binding to PI 4-kinase (Pik1p). Binding studies revealed that Cam2p and the ELC compete for Pik1p. Cortical localization of Cam2p in the myo1 background relied on its association with Pik1p, whereas overexpression studies indicated that Cam2p, in turn, contributes to Pik1p function. The fact that the Myo1p-associated defects of a cam2 mutant are more potent than those of a myo1-IQ2 mutant suggests that myosin light chains can contribute to actomyosin function both directly and indirectly (via phospholipid synthesis at sites of polarized growth).

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“…As in all class I myosins, the tail of Myo1 contains a conserved tail homology domain (TH1 domain), which is required for the association of Myo1 with dynamic lipid regions. The TH1 domain thus permits Myo1-dependent deformation of cellular membranes during endocytosis and, probably, specialised membrane reorganisation during meiosis (Codlin et al, 2008;Itadani et al, 2006;Lee et al, 2000;Takeda and Chang, 2005;Toya et al, 2001).…”

Section: A Class Of Its Own: Myo1mentioning

confidence: 99%

Regulation and function of the fission yeast myosins

East

Mulvihill

2011

Journal of Cell Science

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It is now quarter of a century since the actin cytoskeleton was first described in the fission yeast, Schizosaccharomyces pombe. Since then, a substantial body of research has been undertaken on this tractable model organism, extending our knowledge of the organisation and function of the actomyosin cytoskeleton in fission yeast and eukaryotes in general. Yeast represents one of the simplest eukaryotic model systems that has been characterised to date, and its genome encodes genes for homologues of the majority of actin regulators and actin-binding proteins found in metazoan cells. The ease with which diverse methodologies can be used, together with the small number of myosins, makes fission yeast an attractive model system for actomyosin research and provides the opportunity to fully understand the biochemical and functional characteristics of all myosins within a single cell type. In this Commentary, we examine the differences between the five S. pombe myosins, and focus on how these reflect the diversity of their functions. We go on to examine the role that the actin cytoskeleton plays in regulating the myosin motor activity and function, and finally explore how research in this simple unicellular organism is providing insights into the substantial impacts these motors can have on development and viability in multicellular higher-order eukaryotes.

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Localization of Type I Myosin and F-actin to the Leading Edge Region of the Forespore Membrane in Schizosaccharomyces pombe

Cited by 22 publications

References 41 publications

Live Observation of Forespore Membrane Formation in Fission Yeast

Live Observation of Forespore Membrane Formation in Fission Yeast

A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase

Regulation and function of the fission yeast myosins

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