Degradation of Hof1 by SCFGrr1 is important for actomyosin contraction during cytokinesis in yeast

Blondel, Marc; Bach, Stéphane; Bamps, Sophie; Dobbelaere, Jeroen; Wiget, Philippe; Longaretti, Céline; Barral, Yves; Meijer, Laurent; Peter, Matthias

doi:10.1038/sj.emboj.7600627

Cited by 104 publications

(114 citation statements)

References 54 publications

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“…6c,d and Supplementary Movie 4). Interestingly, this observation matches a report by Blondel et al 42 who replaced the endogenous Hof1 promoter with constitutive CYC1 or ADH promoters and observed that Hof1 started to accumulate shortly after budding, much earlier than when it was expressed from its endogenous promoter. In the experiment we describe here (Fig.…”

Section: Resultssupporting

confidence: 90%

“…As predicted, both proteins are degraded at exactly the same time (52 min after budding). Hof1 (Supplementary Movie 3), transcribed by Ndd1 and degraded by the SCF Grr1 ubiquitin ligase 42 and not by the APC/C Cdh1 , accumulates, as predicted, at the same time as Iqg1. As Hof1 degradation does not depend on the APC/C Cdh1 , it takes place later than that of Iqg1 and Hsl1.…”

Section: Resultssupporting

confidence: 77%

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Degradation of Ndd1 by APC/CCdh1 generates a feed forward loop that times mitotic protein accumulation

et al. 2015

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Ndd1 activates the Mcm1-Fkh2 transcription factor to transcribe mitotic regulators. The anaphase-promoting complex/cyclosome activated by Cdh1 (APC/C Cdh1 ) mediates the degradation of proteins throughout G1. Here we show that the APC/C Cdh1 ubiquitinates Ndd1 and mediates its degradation, and that APC/C Cdh1 activity suppresses accumulation of Ndd1 targets. We confirm putative Ndd1 targets and identify novel ones, many of them APC/C Cdh1 substrates. The APC/C Cdh1 thus regulates these proteins in a dual manner-both pretranscriptionally and post-translationally, forming a multi-layered feedforward loop (FFL). We predict by mathematical modelling and verify experimentally that this FFL introduces a lag between APC/C Cdh1 inactivation at the end of G1 and accumulation of genes transcribed by Ndd1 in G2. This regulation generates two classes of APC/C Cdh1 substrates, early ones that accumulate in S and late ones that accumulate in G2. Our results show how the dual state APC/C Cdh1 activity is converted into multiple outputs by interactions between its substrates.

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Section: Resultssupporting

confidence: 90%

Section: Resultssupporting

confidence: 77%

Degradation of Ndd1 by APC/CCdh1 generates a feed forward loop that times mitotic protein accumulation

et al. 2015

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“…5B). Grr1 and Cdc4 have been reported to be localized in the nucleus (35,36). Together, these findings suggest that Cdc4 and Grr1 are both involved in degradation of processed Stp1, which is predominantly localized in the nucleus.…”

Section: Full-length Stp2 Is More Stable Than Full-length Stp1-mentioning

confidence: 71%

Differential Regulation of Transcription Factors Stp1 and Stp2 in the Ssy1-Ptr3-Ssy5 Amino Acid Sensing Pathway

Tumusiime

Zhang

Overstreet

et al. 2011

Journal of Biological Chemistry

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Stp1 and Stp2 are two homologous transcription factors activated in response to extracellular amino acid stimuli. Here we show that both ubiquitin-dependent degradation of Stp1 and Stp2 and their intracellular localization are differentially regulated. We have found that the E2 ubiquitinconjugating enzyme Cdc34 is required for degradation of both full-length and processed Stp1, but not Stp2. We have also found that Grr1, the F-box component of the SCF Grr1 E3 ubiquitin ligase, is the primary factor in degradation of full-length Stp1, whereas both Grr1 and Cdc4 are required for degradation of processed Stp1. Our localization studies showed that full-length Stp1 is localized both in the cytoplasm and at the cell periphery, whereas full-length Stp2 is localized only diffusely in the cytoplasm. We identified two nuclear localization signals of Stp1 and found that the Nterminal domain of Stp1 is required for localization of fulllength Stp1 to the cell periphery. We also found that Stp2 is the primary factor involved in basal activation of target gene expression. Our results indicate that the functions of two seemingly redundant transcription factors can be separated by differential degradation and distinct cellular localization.

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“…Indeed, its degradation by SCF Grr1 at the end of mitosis is essential for actomyosin ring contraction and cell separation. 29 However, differences do exist between the function of Ataxin-10 and ScHof1. Hof1 is a member of pombe Cdc15 homology (PCH) protein family, which has been shown in many species to regulate actomyosin ring assembly and membrane dynamics, and many of them are involved in actin-based processes.…”

confidence: 99%

Phosphorylation of Ataxin-10 by polo-like kinase 1 is required for cytokinesis

Li¹,

Wang²,

Hou³

et al. 2011

Cell Cycle

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Degradation of Hof1 by SCFGrr1 is important for actomyosin contraction during cytokinesis in yeast

Cited by 104 publications

References 54 publications

Degradation of Ndd1 by APC/CCdh1 generates a feed forward loop that times mitotic protein accumulation

Degradation of Ndd1 by APC/CCdh1 generates a feed forward loop that times mitotic protein accumulation

Differential Regulation of Transcription Factors Stp1 and Stp2 in the Ssy1-Ptr3-Ssy5 Amino Acid Sensing Pathway

Phosphorylation of Ataxin-10 by polo-like kinase 1 is required for cytokinesis

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