Novel<i>sfi1</i>Alleles Uncover Additional Functions for Sfi1p in Bipolar Spindle Assembly and Function

Anderson, Victoria E.; Prudden, John; Prochnik, Simon; Giddings, Thomas H.; Hardwick, Kevin

doi:10.1091/mbc.e06-10-0918

Cited by 28 publications

(40 citation statements)

References 34 publications

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“…8). Sfi1-Cdc31 function is therefore largely conserved between budding and fission yeast (Anderson et al, 2007;Avena et al, 2014;Elserafy et al, 2014). Whereas the SPB duplication function was reported previously (Lee et al, 2014;Paoletti et al, 2003), our data provides the first evidence for a role of Cdc31 in the temporal control of SPB segregation and spindle bipolarity establishment.…”

Section: Discussionsupporting

confidence: 63%

“…Moreover, based on electron microscopy studies, it has been proposed that, to form a half-bridge, these molecules assemble into a parallel array with Sfi1 N-termini attached to the mother SPB. In this model, daughter SPB assembly is initiated by half-bridge duplication, achieved by assembly of a second array of Sfi1 molecules, creating a new half-bridge, anti-parallel to the parental half-bridge and connected to it by interactions between Sfi1 C-termini (Anderson et al, 2007;Li et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Cdk1 phosphorylates the Sfi1 C-terminus to promote the segregation of the two half-bridges at mitotic entry (Anderson et al, 2007;Avena et al, 2014;Elserafy et al, 2014). This event is also controlled to a lesser extent by the polo-like kinase Cdc5 that targets additional sites on the Sfi1 C-terminus (Elserafy et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

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Cell cycle control of spindle pole body duplication and splitting by Sfi1 and Cdc31 in fission yeast

Bouhlel

Ohta

Mayeux

et al. 2015

Journal of Cell Science

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Spindle pole biogenesis and segregation are tightly coordinated to produce a bipolar mitotic spindle. In yeasts, the spindle pole body (SPB) half-bridge composed of Sfi1 and Cdc31 duplicates to promote the biogenesis of a second SPB. Sfi1 accumulates at the half-bridge in two phases in Schizosaccharomyces pombe, from anaphase to early septation and throughout G2 phase. We found that the function of Sfi1-Cdc31 in SPB duplication is accomplished before septation ends and G2 accumulation starts. Thus, Sfi1 early accumulation at mitotic exit might correspond to half-bridge duplication. We further show that Cdc31 phosphorylation on serine 15 in a Cdk1 (encoded by cdc2) consensus site is required for the dissociation of a significant pool of Sfi1 from the bridge and timely segregation of SPBs at mitotic onset. This suggests that the Cdc31 N-terminus modulates the stability of Sfi1-Cdc31 arrays in fission yeast, and impacts on the timing of establishment of spindle bipolarity.

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Section: Discussionsupporting

confidence: 63%

Section: Introductionmentioning

confidence: 99%

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Cell cycle control of spindle pole body duplication and splitting by Sfi1 and Cdc31 in fission yeast

Bouhlel

Ohta

Mayeux

et al. 2015

Journal of Cell Science

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“…1B), Cdc14-D253A pulldown yielded Sfi1. Sfi1 is a component of the SPB half-bridge that is essential for SPB duplication (55,56) and has a role in SPB separation (57). Notably, mutations of a Cdk1 consensus site in the C terminus of Sfi1 prevents separation of duplicated SPBs (57).…”

Section: Figure 2 a Subset Of Cdc14 Interactors Display Enhanced Binmentioning

confidence: 99%

Global Analysis of Cdc14 Phosphatase Reveals Diverse Roles in Mitotic Processes

Bloom

Cristea

Procko

et al. 2011

Journal of Biological Chemistry

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Cdc14 phosphatase regulates multiple events during anaphase and is essential for mitotic exit in budding yeast. Cdc14 is regulated in both a spatial and temporal manner. It is sequestered in the nucleolus for most of the cell cycle by the nucleolar protein Net1 and is released into the nucleus and cytoplasm during anaphase. To identify novel binding partners of Cdc14, we used affinity purification of Cdc14 and mass spectrometric analysis of interacting proteins from strains in which Cdc14 localization or catalytic activity was altered. To alter Cdc14 localization, we used a strain deleted for NET1, which causes full release of Cdc14 from the nucleolus. To alter Cdc14 activity, we generated mutations in the active site of Cdc14 (C283S or D253A), which allow binding of substrates, but not dephosphorylation, by Cdc14. Using this strategy, we identified new interactors of Cdc14, including multiple proteins involved in mitotic events. A subset of these proteins displayed increased affinity for catalytically inactive mutants of Cdc14 compared with the wild-type version, suggesting they are likely substrates of Cdc14. We have also shown that several of the novel Cdc14-interacting proteins, including Kar9 (a protein that orients the mitotic spindle) and Bni1 and Bnr1 (formins that nucleate actin cables and may be important for actomyosin ring contraction) are specifically dephosphorylated by Cdc14 in vitro and in vivo. Our findings suggest the dephosphorylation of the formins may be important for their observed localization change during exit from mitosis and indicate that Cdc14 targets proteins involved in wide-ranging mitotic events.

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“…46,55 These findings and the recurrent finding of small deletion at chromosome 11 strongly suggest a tumor suppressor function of Sfi1.…”

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confidence: 82%

Mutation of C/EBPα predisposes to the development of myeloid leukemia in a retroviral insertional mutagenesis screen

Hasemann

Damgaard

Schuster

et al. 2008

Blood

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Novelsfi1Alleles Uncover Additional Functions for Sfi1p in Bipolar Spindle Assembly and Function

Cited by 28 publications

References 34 publications

Cell cycle control of spindle pole body duplication and splitting by Sfi1 and Cdc31 in fission yeast

Cell cycle control of spindle pole body duplication and splitting by Sfi1 and Cdc31 in fission yeast

Global Analysis of Cdc14 Phosphatase Reveals Diverse Roles in Mitotic Processes

Mutation of C/EBPα predisposes to the development of myeloid leukemia in a retroviral insertional mutagenesis screen

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