Compartmentalized nodes control mitotic entry signaling in fission yeast

Deng, Lin; Moseley, James B.

doi:10.1091/mbc.e13-02-0104

Cited by 38 publications

(71 citation statements)

References 35 publications

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“…However, very interestingly, so far, at least in fission yeast, GBP-tagged proteins have been almost always 'drawn' to GFP-fusion proteins but not the reverse direction, both in our study and published reports (Deng and Moseley, 2013;Dodgson et al, 2013;Grallert et al, 2013). Whether this is due to the strong localization capacity of the tested GFP-fusion proteins or some other unrecognized reasons awaits further investigations on more protein examples.…”

Section: Resultssupporting

confidence: 53%

“…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%

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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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Section: Resultssupporting

confidence: 53%

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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“…However, these interactions do not require Cdr1 kinase activity or the presence of the kinase domain (Deng and Moseley, 2013;Wu and Russell, 1997). Another sharp difference is that Nif1 and Skb1 binding leads to kinase inhibition, indicating that the Cdr1 UBA domain can be classified as an AID.…”

Section: Discussionmentioning

confidence: 97%

Molecular control of the Wee1 regulatory pathway by the SAD kinase Cdr2

Guzmán-Vendrell

Rincón

Dingli

et al. 2015

Journal of Cell Science

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Cell growth and division are tightly coordinated to maintain cell size constant during successive cell cycles. In Schizosaccharomyces pombe, the SAD kinase Cdr2 regulates the cell size at division and the positioning of the division plane. Cdr2 forms nodes on the medial cortex containing factors that constitute an inhibitory pathway for Wee1. This pathway is regulated by polar gradients of the DYRK kinase Pom1, and involves a direct inhibitor of Wee1, the SAD kinase Cdr1. Cdr2 also interacts with the anillin Mid1, which defines the division plane, and with additional components of the medial cortical nodes, including Blt1, which participate in the mitotic-promoting and cytokinetic functions of nodes. Here, we show that the interaction of Cdr2 with Wee1 and Mid1 requires the UBA domain of Cdr2, which is necessary for its kinase activity. In contrast, Cdr1 associates with the C-terminus of Cdr2, which is composed of basic and KA-1 lipid-binding domains. Mid1 also interacts with the C-terminus of Cdr2 and might bridge the N-and C-terminal domains, whereas Blt1 associates with the central spacer region. We propose that the association of Cdr2 effectors with different domains might constrain Cdr1 and Wee1 spatially to promote Wee1 inhibition upon Cdr2 kinase activation.

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“…Pom1 inhibits the Wee1-inhibitory kinases, Cdr1 and Cdr2, which localize to specific nodes at the midcell (Deng and Moseley 2013). As a cell grows, the gradient in Pom1 from the poles ensures that its concentration at the mid-cell decreases, which could allow Cdr1 and Cdr2 to inactivate Wee1 and thereby promote mitotic entry.…”

Section: Geometric Size Sensing In Fission Yeastmentioning

confidence: 99%

Cell-Size Control

Amodeo

Skotheim

2015

Cold Spring Harb Perspect Biol

150

159

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Cells of a given type maintain a characteristic cell size to function efficiently in their ecological or organismal context. They achieve this through the regulation of growth rates or by actively sensing size and coupling this signal to cell division. We focus this review on potential size-sensing mechanisms, including geometric, external cue, and titration mechanisms. Mechanisms that titrate proteins against DNA are of particular interest because they are consistent with the robust correlation of DNA content and cell size. We review the literature, which suggests that titration mechanisms may underlie cell-size sensing in Xenopus embryos, budding yeast, and Escherichia coli, whereas alternative mechanisms may function in fission yeast.

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Compartmentalized nodes control mitotic entry signaling in fission yeast

Abstract: The conserved fission yeast protein Skb1 inhibits mitotic entry through the SAD kinase Cdr1. Skb1 and Cdr1 are spatially segregated in discrete sets of stable nodes at the cell cortex. This work reveals new spatial control elements of the mitotic size control system.

Cited by 38 publications

References 35 publications

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

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

Molecular control of the Wee1 regulatory pathway by the SAD kinase Cdr2

Cell-Size Control

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