Pom1 regulates the assembly of Cdr2–Mid1 cortical nodes for robust spatial control of cytokinesis

Rincón, Sergio A.; Bhatia, Payal; Bicho, Claudia C.; Guzmán-Vendrell, Mercè; Fraisier, Vincent; Borek, Weronika E.; Alves, Flávia de Lima; Dingli, Florent; Loew, Damarys; Rappsilber, Juri; Sawin, Kenneth E.; Martin, Sophie G.; Paoletti, Anne

doi:10.1083/jcb.201311097

Cited by 59 publications

(95 citation statements)

References 70 publications

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“…This family contains classical AMPKs (Ucp9, also known as Ssp2, in fission yeast) as well as a series of closely related kinases including the MARK kinases (Kin1 in fission yeast) and the SAD or BRSK kinases (Cdr2 and Cdr1 in fission yeast). AMPK-like kinases share a series of structural features including an N-terminal serine/ threonine kinase domain associated with a ubiquitin-associated (UBA) domain or auto inhibitory domain (AID), a medial spacer and a C-terminal lipid-binding KA-1 domain (Marx et al, 2010;Moravcevic et al, 2010;Rincon et al, 2014).…”

Section: Resultsmentioning

confidence: 99%

“…pSR160 (described in Rincon et al, 2014) was produced by amplification of cdr2 from codon 591 to 747 with oligonucleotides containing XhoI ( plus an ATG codon) and NotI sites, and cloning into a pJK148 plasmid containing the cdr2 promoter, a C-terminal Myc 12 tag derived from pINV-Myc (Iacovoni et al, 1999) and the nmt1 terminator. The plasmid was digested with NruI before transformation.…”

Section: -330mentioning

confidence: 99%

“…In the same way, the plasmids containing C-terminal fragments ( pSR45, pSR46 and pSR156) were obtained by amplification of cdr2 from the codon 531, 591 or 331, respectively, to the last codon with oligonucleotides containing a BamHI site plus an ATG codon and a PacI site, and cloning into pSR20. pSR25 (described in Rincon et al, 2014) was produced by amplification of cdr2 from codon 591 to 747 with oligonucleotides containing the PacI and AscI sites plus the stop codon TAA, and cloning in frame after an EGFP tag in the pSR20 plasmid.…”

Section: Cdr2 Integration Plasmidsmentioning

confidence: 99%

“…Inhibition of Cdr2 activity depends on the phosphorylation, by Pom1, of an autoinhibitory tail which can block the phosphorylation of Cdr2 T-loop on T166 by the stress kinase Ssp1, which is required for the activation of the kinase domain. Pom1 independently restricts Cdr2 node assembly to the medial cortex by reducing the membrane-binding affinity and clustering properties of Cdr2 in the cell tips where Pom1 concentration is high Deng et al, 2014;Rincon et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

Section: -330mentioning

confidence: 99%

Section: Cdr2 Integration Plasmidsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…2C). These inhibitory gradients help guide accumulation of division initiators at midcell Pan et al 2014;Rincon et al 2014). A somewhat similar mechanism operates in Escherichia coli, where the MinCDE system relies on an oscillatory pattern of division inhibitor localization at the two cell poles (Hu et al 1999;Raskin and de Boer 1999).…”

Section: Intracellular Scaling Mechanismsmentioning

confidence: 97%

Intracellular Scaling Mechanisms

Reber

Goehring

2015

Cold Spring Harb Perspect Biol

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Organelle function is often directly related to organelle size. However, it is not necessarily absolute size but the organelle-to-cell-size ratio that is critical. Larger cells generally have increased metabolic demands, must segregate DNA over larger distances, and require larger cytokinetic rings to divide. Thus, organelles often must scale to the size of the cell. The need for scaling is particularly acute during early development during which cell size can change rapidly. Here, we highlight scaling mechanisms for cellular structures as diverse as centrosomes, nuclei, and the mitotic spindle, and distinguish them from more general mechanisms of size control. In some cases, scaling is a consequence of the underlying mechanism of organelle size control. In others, size-control mechanisms are not obviously related to cell size, implying that scaling results indirectly from cell-size-dependent regulation of sizecontrol mechanisms.

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From Structure to Function: A Comprehensive Compendium of Tools to Unveil Protein Domains and Understand Their Role in Cytokinesis

Rincón

Paoletti

2016

Methods in Molecular Biology

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Unveiling the function of a novel protein is a challenging task that requires careful experimental design. Yeast cytokinesis is a conserved process that involves modular structural and regulatory proteins. For such proteins, an important step is to identify their domains and structural organization. Here we briefly discuss a collection of methods commonly used for sequence alignment and prediction of protein structure that represent powerful tools for the identification homologous domains and design of structure-function approaches to test experimentally the function of multi-domain proteins such as those implicated in yeast cytokinesis.

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Pom1 regulates the assembly of Cdr2–Mid1 cortical nodes for robust spatial control of cytokinesis

Abstract: Pom1 regulation of Cdr2 membrane association and interaction with Mid1 prevents Cdr2 assembly into stable nodes in the cell tip region, which ensures proper positioning of cytokinetic ring precursors and accurate division plane positioning in fission yeast.

Cited by 59 publications

References 70 publications

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

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

Intracellular Scaling Mechanisms

From Structure to Function: A Comprehensive Compendium of Tools to Unveil Protein Domains and Understand Their Role in Cytokinesis

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