A cyclin B homolog in S. cerevisiae: Chronic activation of the Cdc28 protein kinase by cyclin prevents exit from mitosis

Ghiara, J.B.; Richardson, Helena E.; Sugimoto, Katsunori; Henze, Martha; Lew, Daniel J.; Wittenberg, Curt; Reed, Steven I.

doi:10.1016/0092-8674(91)90417-w

Cited by 299 publications

(253 citation statements)

References 66 publications

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“…These findings have led to the notion that cyclin destruction (and thereby kinase inactivation) triggers the metaphase to anaphase transition (Murray and Kirschner, 1989; Glotzer et al, 1991). However, apart from a single preliminary study (Ghiara et al, 1991) (Ghiara et al, 1991;Surana et al, 1991) Of these, CLB2 seems the most important for mitosis because its deletion uniquely delays exit from G2 whereas triple mutants lacking CLBI, 3 and 4 undergo nuclear division with nearly normal kinetics (Fitch et al, 1992). We show here that CDC28 kinase activity associated with CLB2 fluctuates during the cell cycle, reaching a maximum just prior to anaphase and disappearing soon after.…”

Section: Introductionmentioning

confidence: 99%

Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast.

et al. 1993

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It is widely assumed that degradation of mitotic cyclins causes a decrease in mitotic cdc2/CDC28 kinase activity and thereby triggers the metaphase to anaphase transition. Two observations made on the budding yeast Saccharomcyces cerevisiae are inconsistent with this scenario: (i) anaphase occurs in the presence of high levels of kinase in cdc15 mutants and (ii) overproduction of a B-type mitotic cyclin causes arrest not in metaphase as previously reported but in telophase. Kinase destruction is therefore implicated in the exit from mitosis rather than the entry into anaphase. The behaviour of espi mutants shows in addition that kinase destruction can occur in the absence of anaphase completion. The execution of anaphase and the destruction of CDC28 kinase activity therefore appear to take place independently of one another.

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Section: Introductionmentioning

confidence: 99%

Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast.

et al. 1993

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“…It has been proposed that some checkpoint controls over mitosis are switched from the APC/C during G1 to include tyrosine phosphorylation of p34 cdc2 upon initiation of DNA replication (Ye et al, 1997a). BIME APC1 may therefore normally play a role to prevent activation of NIMA kinase, and other mitotic regulators, during interphase to prevent premature mitosis.The levels of NIME cyclinB and NIMA proteins oscillate once each cell cycle in a strikingly similar manner (Evans et al, 1983;Alfa et al, 1990;Draetta et al, 1990;Ghiara et al, 1991;Hunt et al, 1992;Richardson et al, 1992;Grandin and Reed, 1993;Pu and Osmani, 1995;Ye et al, 1995;Yamano et al, 1996). Both proteins accumulate during late S to G2, peak at early M, and are rapidly degraded as cells progress out of mitosis with slightly different kinetics Ye et al, 1995).…”

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Regulation of the Anaphase-promoting Complex/Cyclosome bybimA^APC3and Proteolysis of NIMA

Fincher

Tang

et al. 1998

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Surprisingly, although highly temperature-sensitive, the bimA1 APC3 anaphase-promoting complex/cyclosome (APC/C) mutation does not cause arrest of mitotic exit. Instead, rapid inactivation of bimA1 APC3 is shown to promote repeating oscillations of chromosome condensation and decondensation, activation and inactivation of NIMA and p34 cdc2 kinases, and accumulation and degradation of NIMA, which all coordinately cycle multiple times without causing nuclear division. These bimA1 APC3 -induced cell cycle oscillations require active NIMA, because a nimA5 ϩ bimA1 APC3 double mutant arrests in a mitotic state with very high p34 cdc2 H1 kinase activity. NIMA protein instability during S phase and G2 was also found to be controlled by the APC/C. The bimA1 APC3 mutation therefore first inactivates the APC/C but then allows its activation in a cyclic manner; these cycles depend on NIMA. We hypothesize that bimA APC3 could be part of a cell cycle clock mechanism that is reset after inactivation of bimA1 APC3 . The bimA1 APC3 mutation may also make the APC/C resistant to activation by mitotic substrates of the APC/C, such as cyclin B, Polo, and NIMA, causing mitotic delay. Once these regulators accumulate, they activate the APC/C, and cells exit from mitosis, which then allows this cycle to repeat. The data indicate that bimA APC3 regulates the APC/C in a NIMA-dependent manner. INTRODUCTIONThe bimE and bimA genes were originally defined by temperature-sensitive mutations in functions required for normal progression through mitosis in Aspergillus nidulans (Morris, 1976;Osmani et al., 1988;Engle et al., 1990;O'Donnell et al., 1991) and were subsequently found to encode highly conserved proteins whose homologues have been isolated from many organisms ranging from fungi to humans (Hirano et al., 1990(Hirano et al., , 1994Mirabito and Morris, 1993;Lamb et al., 1994;Starborg et al., 1994;King et al., 1995;. Most significantly, they were recently identified as components of the anaphase-promoting complex (APC) (King et al., 1995;Peters et al., 1996;. The APC is also known as the cyclosome and is therefore abbreviated here to APC/C (see Townsley and Ruderman, 1998, for review).bimE encodes the largest subunit of the APC/C and has recently been termed APC1 . We will use the designation bimE APC1 for the gene and BIME APC1 for the protein. bimA encodes a member of the tetratricopeptide repeat family of proteins, being most similar to Schizosaccharomyces pombe nuc2 (Hirano et al., 1990(Hirano et al., , 1994 and Saccharomyces cerevisiae CDC27 (Sikorski et al., 1990;Lamb et al., 1994), which was recently termed APC3 APC/C functions as an E3 ubiquitin ligase, which specifically targets proteins (such as mitotic cyclins) for degradation in a destruction box (D box)-dependent manner (Glotzer et al., 1991;King et al., 1996b) through the ubiquitin-proteasome pathway, to promote initiation of anaphase and exit from mitosis into G1 (for reviews see Murray, 1995;King et al., 1996a;Hershko, 1997;Townsley and Ruderman, 1998). APC/C activity i...

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“…Cdc2 is positively regulated by cyclin B (Pines and Hunter, 1989;Ghiara et al, 1991;Surana et al, 1991). The binding of cyclin B to Cdc2 induces phosphorylation of the complex, which leads to its activation at the G2 to M transition (Enoch and Nurse, 1990;Gould et al, 1991).…”

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Functional association of TGF-β receptor II with cyclin B

et al. 1999

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Utilizing the cytoplasmic tail of Transforming Growth Factor Receptor Type II (TGFb RII) as bait in a yeast two hybrid system, we have identi®ed human cyclin B2 as a direct physical partner of TGFb RII. Analysis of deletion mutants of glutathione-S-transferase (GST)-cyclin B2 mapped its binding domain for TGFb RII to the C-terminal and revealed a negative regulatory region immediately upstream of the cyclin box. Using recombinant proteins, Cdc2 was demonstrated to indirectly interact with TGFb RII via cyclin B2. This interaction was reproduced in THP-1 monocytic cells, where TGFb treatment markedly enhanced the ability of cyclin B2 and, correspondingly, Cdc2 from TGFb-treated THP-l cells, to bind the GST-TGFb RII fusion protein. More importantly, TGFb RII co-precipitated with cyclin B2 in TGFb-treated THP-1 cells. TGFb treatment also caused threonine phosphorylation of Cdc2 in the TGFb RIIcyclin B2-Cdc2 complex in THP1 cells, in parallel with down regulation of Cdc2 function as measured by histone H1 kinase activity. Cyclin B1 had the same capacity to bind TGFb RII and mediate indirect Cdc2 binding. These results suggest an alternative mechanism that cell cycle arrest in the G1/S phase caused by TGFb may, in part, be due to inactivation of cyclin B/Cdc2 kinase, which is needed for entry into the G2/M phase.

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A cyclin B homolog in S. cerevisiae: Chronic activation of the Cdc28 protein kinase by cyclin prevents exit from mitosis

Cited by 299 publications

References 66 publications

Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast.

Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast.

Regulation of the Anaphase-promoting Complex/Cyclosome bybimA^APC3and Proteolysis of NIMA

Functional association of TGF-β receptor II with cyclin B

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A cyclin B homolog in S. cerevisiae: Chronic activation of the Cdc28 protein kinase by cyclin prevents exit from mitosis

Cited by 299 publications

References 66 publications

Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast.

Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast.

Regulation of the Anaphase-promoting Complex/Cyclosome bybimAAPC3and Proteolysis of NIMA

Functional association of TGF-β receptor II with cyclin B

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Regulation of the Anaphase-promoting Complex/Cyclosome bybimA^APC3and Proteolysis of NIMA