The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae

Schwob, Étienne; Böhm, Thomas; Mendenhall, Michael J.; Nasmyth, Kim

doi:10.1016/0092-8674(94)90193-7

Cited by 874 publications

(848 citation statements)

References 39 publications

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“…Our present results do not exclude the possibility that Z-Phe-Ser-argininal inhibits the degradation process of cdk inhibitors in addition to the dephosphorylation process, since several lines of evidence indicate the participation of proteasome in degradation of cdk inhibitors (13,14). However, as reported previously (5), Z-Phe-Ser-argininal strongly inhibits the GVBD but not the polar body extrusion or egg cleavage.…”

Section: Discussioncontrasting

confidence: 50%

“…In addition, it is also unclear whether the increase in MPF activity is derived from the dephosphorylation of Tyrl5 of cdc2 kinase or from some other processes including the possible degradation of cyclin-dependent kinase (cdk) inhibitors, since it has recently been revealed that several cdk-inhibitors are degraded by the proteasome in a ubiquitin/ATP-dependent manner (13,14).…”

Section: Biochemistry and Molecular Biology Internationalmentioning

confidence: 99%

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Protease triggers dephosphorylation of cdc2 kinase during starfish oocyte maturation

et al. 1997

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Summary: We previously presented evidence that a Z-Phe-Ser-argininal-susceptible protease which is involved in oocyte maturation of the starfish, Asterina pectinifera is the proteasome (Takagi Sawada et al., Dev. BioL 150, 414-418 (1992)). In the present study, we investigated the timing of the function of and the role of the protease in oocyte maturation using Z-Phe-Ser-argininal. By adding the inhibitor in maturing oocytes at various times after 1-methyladenine treatment, the inhibitory ability was markedly reduced in half the time required for germinal vesicle breakdown. Furthermore, the inhibitor potently blocked the activation of histone H 1 kinase and the dephosphorylation of cdc2 kinase during oocyte maturation. These results indicate that the Z-Phe-Ser-argininalsusceptible protease, probably the proteasome, plays a key role in the step of the signal transduction pathway that triggers the dephosphorylation of cdc2 kinase in response to the maturation-inducing hormone.

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Section: Discussioncontrasting

confidence: 50%

Section: Biochemistry and Molecular Biology Internationalmentioning

confidence: 99%

Protease triggers dephosphorylation of cdc2 kinase during starfish oocyte maturation

et al. 1997

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“…Interestingly, we found that Erk1 phosphorylated p27 is in agreement with the fact that in S. cerevisi , p40 Sic1 , an ( Figure 1a, lane 2), exclusively on serine (Figure 1b, lane 1) inhibitor of yeast Cdks, accumulates in ubc3/cdc34 mutant suggesting that this kinase might be involved in the in vivo cells. Deletion of the sic1 gene allows entry into S-phase, 50 phosphorylation of p27. suggesting that the G1 arrest caused by inactivation of In summary, p27 abundance is regulated by ubiquitinUbc3/Cdc34 in G1 is due to a failure to destroy p40 Sic1 .…”

Section: Regulation Of the Cyclin-dependent Kinase Inhibitor P27mentioning

confidence: 99%

Regulation of the cyclin-dependent kinase inhibitor p27 by degradation and phosphorylation

1997

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The cell cycle has been the object of extensive studies for the in vitro. [21][22][23] It was subsequently cloned and found to be able past years. A complex network of molecular interactions has to block mammalian cells in the G1 phase of the cell cycle been identified. In particular, a class of cell cycle inhibitory prowhen overexpressed. 17,18 teins has been cloned and characterized but details of the molCkis have been suggested as the products of potential antiecular mechanism of their action have yet to be resolved. These oncogenes since their function is often missing in tumor cells. ation by these kinases is involved in the process of p27 proteop27 protein is expressed at higher levels in quiescent cells lysis.than in proliferating cells. [36][37][38][39] In addition, p27 abundance Keywords: cell cycle; cyclin dependent-kinase inhibitors; p27; tumor suppressors; ubiquitination increases in cells treated with cAMP, 40 tamoxifen, 41 lovastatin, 23 or rapamycin. 37 This increase is thought to be involved in the G1 block induced by these agents. Similarly, cells The eukaryotic cell division cycle is a highly ordered series undergoing differentiation have elevated levels of p27. 42-44 of events, regulated by a number of cyclin dependent kinases Interestingly, levels of p27 mRNA do not change in any of the (Cdks), each consisting of a regulatory cyclin subunit and a analyzed conditions. catalytic serine/threonine kinase subunit (for a review, see Ref.The contrast between oscillation of p27 protein abundance 1). Several cyclin-Cdk complexes have been identified and and the constant amounts of its mRNA observed at different found to be required at different stages of the cell cycle. There cell cycle phases prompted us to determine whether p27 halfare several distinct molecular mechanisms for controlling the life was chronologically regulated by alterations of protein activity of the different Cdks: regulated synthesis and destrucstability. 45 We found that the half-life of p27 is much longer tion of the cyclin regulatory subunit; post-translational modiin quiescent than in proliferating cells. This result led us to fication of the kinase subunit by highly specific kinases and investigate the mechanisms regulating p27 degradation. 45 phosphatases, and association/dissociation with a variety of Ubiquitin is a MW 7000 protein which is covalently bound inhibitory proteins (reviewed in Ref. 2).through an isopeptide bond to a target protein, forming a polyBased on sequence homology and specificity of interaction ubiquitin tree (see Refs 46 and 47 for a review). This reaction with Cdks, two families of inhibitors (ckis) have been identis catalyzed by the ubiquitinating enzymes E1, E2s and E3s. ified in mammalian cells (for a review, see Ref.3). The first E1, also called ubiquitin activating enzyme, is the first enzyme family includes p16 (also called Ink4A, Mts1, Cdkn2 and involved in protein ubiquitination. It forms a thioester bond Cdk4i 4,5 ), p15 (also called Ink4B, Mts2 5-8 ) p18 (also called between the C-terminus...

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“…Nasmyth and Hunt (1993) have suggested that Cdks`build up like water behind a CKI dam,' and that over¯ow of Cdk from the dam triggers proteolysis or inactivation of the CKI, releasing a¯ood of Cdks that irrevocably commit the cell to the next phase of the cell cycle. Several CKIs appear to be regulated by proteolysis (McKinney et al, 1993;Schwob et al, 1994;Pagano et al, 1995), and while mechanisms for rapidly activating the proteolysis have not been generally demonstrated, Sherr (1996) cites a report that Cdk2/cyclin E accelerates turnover of p27 Kip1 . If a Cdk activates CKI proteolysis this releases more Cdk, creating positive feedback and possibly leading to complete destruction of CKI and a stable state with CKI obliterated and Cdk freed.…”

Section: Introductionmentioning

confidence: 99%

Bistable biochemical switching and the control of the events of the cell cycle*

Thron

1997

Oncogene

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The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae

Cited by 874 publications

References 39 publications

Protease triggers dephosphorylation of cdc2 kinase during starfish oocyte maturation

Protease triggers dephosphorylation of cdc2 kinase during starfish oocyte maturation

Regulation of the cyclin-dependent kinase inhibitor p27 by degradation and phosphorylation

Bistable biochemical switching and the control of the events of the cell cycle*

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