Distinct molecular mechanism regulate cell cycle timing at successive stages of Drosophila embryogenesis.

Edgar, Brace A.; Sprenger, Frank; Duronio, Robert J.; Léopold, Pierre; O’Farrell, Patrick H.

doi:10.1101/gad.8.4.440

Cited by 287 publications

(378 citation statements)

References 69 publications

(66 reference statements)

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“…In Drosophila and Xenopus, inhibitory phosphorylation is not detected during these rapid cycles 14,42 . Despite the lack of detected inhibitory phosphorylation in frog eggs, it is detected in cycling extracts prepared from these eggs.…”

Section: Invisible Inhibitory Phosphorylationmentioning

confidence: 96%

“…During G2, the cyclin:Cdk1 of S. pombe, Drosophila, vertebrates, echinoderms and plants is held inactive by inhibitory phosphorylation of residues Y15 and T14 of Cdk1 [12][13][14][15][16][17] . Maintenance of this inhibitory phosphorylation is required for G2 quiescence [18][19][20] .…”

Section: Controlling Inhibitory Phosphorylation Of Cdk1mentioning

confidence: 99%

“…In addition, Chk1-and Wee1-stimulated phosphorylation promotes cell cycle arrest in fly embryos and in a frog embryonic extract system upon inhibition of DNA replication 43,44 . Importantly, Chk1 grapes and Wee1 function are required to regulate the normal progression of the early embryonic cycles that exhibit no inhibitory phosphorylation 14,27,44 . Hence, inhibitory phosphorylation of a small fraction of Cdk1, presumably a special and perhaps nuclear pool, appears to be required for the regulation of these cycles 45 .…”

Section: Invisible Inhibitory Phosphorylationmentioning

confidence: 99%

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Triggering the all-or-nothing switch into mitosis

O’Farrell

2001

Trends in Cell Biology

168

147

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The past decade of cell cycle investigations has identified many roads not taken. The kinase that drives mitosis can be modulated by cyclins, by activating phosphorylation, by inhibitory phosphorylation and by binding of inhibitors, but one of these regulatory options controls the transition from G2 phase to mitosis in most circumstances. A switch-like mechanism integrates signals of cellular status and commits the cell to mitosis by abruptly removing inhibitory phosphate from preformed cyclin:Cdk1 complexes. The pathways that flip this switch alter the balance of modifying reactions to favor dephosphorylation, thereby generating a flood of mitotic kinase.

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Section: Invisible Inhibitory Phosphorylationmentioning

confidence: 96%

Section: Controlling Inhibitory Phosphorylation Of Cdk1mentioning

confidence: 99%

Section: Invisible Inhibitory Phosphorylationmentioning

confidence: 99%

See 1 more Smart Citation

Triggering the all-or-nothing switch into mitosis

O’Farrell

2001

Trends in Cell Biology

168

147

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“…In contrast, the phosphorylated (upper) isoforms of Cdc2 are inactive and dephosphorylation leading to activation causes a shift to a lower band. Abundant monomeric inactive Cdc2 also migrates in the lower band (Edgar et al, 1994;Pérez-Mongiovi et al, 2000). Because our extracts were made at a time corresponding to the beginning of mitosis, most CyclinB is nonphosphorylated and present in the inactive pre-MPF complex, containing inactive phosphorylated Cdc2.…”

Section: Compartmentalisation Of Active and Inactive Cdc25c And Mpfmentioning

confidence: 99%

Pre-M Phase-promoting Factor Associates with Annulate Lamellae inXenopusOocytes and Egg Extracts

Beckhelling

Chang

Chevalier

et al. 2003

MBoC

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We have used complementary biochemical and in vivo approaches to study the compartmentalization of M phase-promoting factor (MPF) in prophase Xenopus eggs and oocytes. We first examined the distribution of MPF (Cdc2/CyclinB2) and membranous organelles in high-speed extracts of Xenopus eggs made during mitotic prophase. These extracts were found to lack mitochondria, Golgi membranes, and most endoplasmic reticulum (ER) but to contain the bulk of the pre-MPF pool. This pre-MPF could be pelleted by further centrifugation along with components necessary to activate it. On activation, Cdc2/CyclinB2 moved into the soluble fraction. Electron microscopy and Western blot analysis showed that the pre-MPF pellet contained a specific ER subdomain comprising "annulate lamellae" (AL): stacked ER membranes highly enriched in nuclear pores. Colocalization of pre-MPF with AL was demonstrated by anti-CyclinB2 immunofluorescence in prophase oocytes, in which AL are positioned close to the vegetal surface. Green fluorescent protein-CyclinB2 expressed in oocytes also localized at AL. These data suggest that inactive MPF associates with nuclear envelope components just before activation. This association may explain why nuclei and centrosomes stimulate MPF activation and provide a mechanism for targeting of MPF to some of its key substrates. INTRODUCTIONThe structural changes accompanying mitosis and meiosis are governed in almost all species by M phase-promoting factor (MPF) (Masui and Markert, 1971), a complex of Cyclin B and the kinase Cdc2 (reviewed in Nigg, 1995;Morgan, 1997). Direct and indirect targets for MPF include the nuclear envelope and lamina, chromatin proteins, and regulators of mitotic spindle formation (Moreno and Nurse, 1990;Norbury and Nurse, 1992). MPF activation requires the continuous synthesis and accumulation during interphase of Cyclin B, which binds Cdc2 to form inactive pre-MPF. Pre-MPF is maintained inactive by inhibitory phosphorylation on Cdc2 by the Wee1 and Myt1 kinases. At the onset of mitosis, rapid MPF activation is favored by a positive feedback loop involving Cdc25 phosphatases, MPF itself, and Polo-like kinases. Degradation of Cyclin B at the metaphaseto-anaphase transition by the anaphase promoting complex (APC) destroys the MPF complex and causes exit from mitosis (reviewed in Nurse, 1990; Whitaker and Patel., 1990;Norbury and Nurse, 1992;Nigg, 1995;Morgan, 1997Morgan, , 1999Beckhelling and Ford, 1998;O'Farrell, 2001).Amphibian eggs have proved extremely useful for the study of MPF regulation. Cycles of Cyclin B accumulation and destruction sufficient to drive synchronous cell cycles in the absence of any other protein synthesis occur in both fertilized or activated eggs and in egg extracts (Murray and Kirschner, 1989;Hartley et al., 1996). Although MPF activation cycles in amphibian oocytes and eggs can continue in the absence of nuclei and microtubules (Hara et al., 1980;Shinagawa, 1983;Gerhart et al., 1984;Newport and Kirschner, 1984;Kimelman et al., 1987;Shinagawa, 1992) both in manipulate...

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“…Like Twine, the String half-life also changes from 20 min to 5 min between the early cleavage embryo and the MBT, but this change is gradual and begins well before the MBT. 17,18,23 Key to this degradation is the Chk1 kinase ortholog Grapes, 24 which appears to require zygotic transcription to be activated (Fig. 2).…”

Section: The Midblastula Transition: Introducing Cell Cycle Complexitmentioning

confidence: 99%

Cdc25 and the importance of G₂control

Bouldin¹,

Kimelman

2014

Cell Cycle

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Distinct molecular mechanism regulate cell cycle timing at successive stages of Drosophila embryogenesis.

Cited by 287 publications

References 69 publications

Triggering the all-or-nothing switch into mitosis

Triggering the all-or-nothing switch into mitosis

Pre-M Phase-promoting Factor Associates with Annulate Lamellae inXenopusOocytes and Egg Extracts

Cdc25 and the importance of G₂control

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Distinct molecular mechanism regulate cell cycle timing at successive stages of Drosophila embryogenesis.

Cited by 287 publications

References 69 publications

Triggering the all-or-nothing switch into mitosis

Triggering the all-or-nothing switch into mitosis

Pre-M Phase-promoting Factor Associates with Annulate Lamellae inXenopusOocytes and Egg Extracts

Cdc25 and the importance of G2control

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Cdc25 and the importance of G₂control