Spatial segregation of polarity factors into distinct cortical clusters is required for cell polarity control

Dodgson, James; Chessel, Anatole; Yamamoto, Miki; Vaggi, Federico; Cox, Susan; Rosten, Edward; Albrecht, David; Geymonat, Marco; Csikász‐Nagy, Attila; Sato, Masamitsu; Carazo-Salas, Rafael E.

doi:10.1038/ncomms2813

Cited by 54 publications

(50 citation statements)

References 43 publications

(57 reference statements)

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“…This is consistent with the recent observation that polarity factors are spatially segregated into distinct clusters on the cell surface in both S. pombe and S. cerevisiae (Dodgson et al 2013). Although some of these features vary across different growth forms (i.e., yeast cells vs. hyphae), they appear to be universally coordinated by Cdc42/Rho1-related GTPase modules and their numerous effectors.…”

supporting

confidence: 90%

Fungal Morphogenesis

Lin

Alspaugh

Liu

et al. 2014

Cold Spring Harbor Perspectives in Medicine

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Morphogenesis in fungi is often induced by extracellular factors and executed by fungal genetic factors. Cell surface changes and alterations of the microenvironment often accompany morphogenetic changes in fungi. In this review, we will first discuss the general traits of yeast and hyphal morphotypes and how morphogenesis affects development and adaptation by fungi to their native niches, including host niches. Then we will focus on the molecular machinery responsible for the two most fundamental growth forms, yeast and hyphae. Last, we will describe how fungi incorporate exogenous environmental and host signals together with genetic factors to determine their morphotype and how morphogenesis, in turn, shapes the fungal microenvironment. PROPERTIES OF MORPHOGENESIS IN FUNGAL CELLS

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supporting

confidence: 90%

Fungal Morphogenesis

Lin

Alspaugh

Liu

et al. 2014

Cold Spring Harbor Perspectives in Medicine

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“…A 13-kDa soluble protein derived from a llama heavy chain antibody (called GFP-binding protein or GBP) has been recently developed for protein targeting in vivo (Rothbauer et al, 2006(Rothbauer et al, , 2008 and rapidly applied to cultured mammalian cells and various model organisms, including fly, worm, Nicotiana, Arabidopsis and S. pombe (Deng and Moseley, 2013;Dodgson et al, 2013;Grallert et al, 2013;Maier et al, 2013;Neumuller et al, 2012;Qu et al, 2013;Rothbauer et al, 2008;Schornack et al, 2009;Sonneville et al, 2012;Tao et al, 2014;Ye et al, 2012). This single-domain antibody features has high binding affinity to GFP as well as to some GFP variants, such as yellow fluorescent protein (YFP), with a stoichiometric ratio of 1:1, but not to cyan fluorescent protein (CFP) or any derivatives of DsRed, such as mRFP, mCherry or mOrange (Kirchhofer et al, 2010;Kubala et al, 2010;Rothbauer et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Facile manipulation of protein localization in fission yeast through binding of GFP-binding protein to GFP

Chen

Wang

Hao

et al. 2017

Journal of Cell Science

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GFP-binding protein (or GBP) has been recently developed in various systems and organisms as an efficient tool to purify GFP-fusion proteins. Due to the high affinity between GBP and GFP or GFP variants, this GBP-based approach is also ideally suited to alter the localization of functional proteins in live cells. In order to facilitate the wide use of the GBP-targeting approach in the fission yeast Schizosaccharomyces pombe, we developed a set of pFA6a-, pJK148-and pUC119-based vectors containing GBP-or GBPmCherry-coding sequences and variants of inducible nmt1 or constitutive adh1 promoters that result in different levels of expression. The GBP or GBP-mCherry fragments can serve as cassettes for N-or C-terminal genomic tagging of genes of interest. We illustrated the application of these vectors in the construction of yeast strains with Dma1 or Cdc7 tagged with GBP-mCherry and efficient targeting of Dma1-or Cdc7-GBP-mCherry to the spindle pole body by Sid4-GFP. This series of vectors should help to facilitate the application of the GBP-targeting approach in manipulating protein localization and the analysis of gene function in fission yeast, at the level of single genes, as well as at a systematic scale.

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“…A possible explanation is provided by the observation that the chimera proteins appear (partly) clustered in the membrane (Fig. 3C), as do many natural polarity factors in fission yeast (27). If this clustering, and subsequent slow diffusion, is in some way promoted by the increase in protein concentration near or at microtubule tips, then this may lead to a diffusive concentration gradient extending beyond the region of microtubule tip-cortex contacts, assuming that the locally created slow diffusing species eventually converts back to a fast diffusing species (see also the discussion of Fig.…”

Section: A Model For Polarization Based On Membrane Binding and Micromentioning

confidence: 99%

Chimera proteins with affinity for membranes and microtubule tips polarize in the membrane of fission yeast cells

Recouvreux

Sokolowski

Γραμμουστιάνου

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Cell polarity refers to a functional spatial organization of proteins that is crucial for the control of essential cellular processes such as growth and division. To establish polarity, cells rely on elaborate regulation networks that control the distribution of proteins at the cell membrane. In fission yeast cells, a microtubule-dependent network has been identified that polarizes the distribution of signaling proteins that restricts growth to cell ends and targets the cytokinetic machinery to the middle of the cell. Although many molecular components have been shown to play a role in this network, it remains unknown which molecular functionalities are minimally required to establish a polarized protein distribution in this system. Here we show that a membrane-binding protein fragment, which distributes homogeneously in wild-type fission yeast cells, can be made to concentrate at cell ends by attaching it to a cytoplasmic microtubule end-binding protein. This concentration results in a polarized pattern of chimera proteins with a spatial extension that is very reminiscent of natural polarity patterns in fission yeast. However, chimera levels fluctuate in response to microtubule dynamics, and disruption of microtubules leads to disappearance of the pattern. Numerical simulations confirm that the combined functionality of membrane anchoring and microtubule tip affinity is in principle sufficient to create polarized patterns. Our chimera protein may thus represent a simple molecular functionality that is able to polarize the membrane, onto which additional layers of molecular complexity may be built to provide the temporal robustness that is typical of natural polarity patterns.

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Spatial segregation of polarity factors into distinct cortical clusters is required for cell polarity control

Cited by 54 publications

References 43 publications

Fungal Morphogenesis

Fungal Morphogenesis

Facile manipulation of protein localization in fission yeast through binding of GFP-binding protein to GFP

Chimera proteins with affinity for membranes and microtubule tips polarize in the membrane of fission yeast cells

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