The Polo-related kinase Cdc5 activates and is destroyed by the mitotic cyclin destruction machinery in S. cerevisiae

Charles, Julia F.; Jaspersen, Sue L.; Tinker-Kulberg, Rachel; Hwang, Lena H.; Szidon, Alex; Morgan, David

doi:10.1016/s0960-9822(98)70201-5

Cited by 222 publications

(247 citation statements)

References 67 publications

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“…Mitotic degradation of other regulatory proteins (Cohen-Fix et al, 1996;Funabiki et al, 1996;Juang et al, 1997;Michaelis et al, 1997;Charles et al, 1998;Shirayama et al, 1998) is also required for normal exit from mitosis, and these proteins are . 10, 13, 32, 76, 109, and 131 are deletions in GR5, and 19R and 30R indicate deletions in a bimE7 APC1 strain.…”

Section: Discussionmentioning

confidence: 99%

“…Of course it is possible that both p34 cdc2 /cyclin B and NIMA are involved in the activation of the APC/C at mitosis, along with other regulators such as Polo-like kinases (Charles et al, 1998;Descombes and Nigg, 1998;Shirayama et al, 1998). The important point is that bimA APC3 apparently plays a regulatory role in APC/C function.…”

Section: Discussionmentioning

confidence: 99%

“…APC/C activity is cell cycle regulated (Hershko et al, 1994; potentially by reversible phosphorylation (Lahav-Baratz et al, 1995) of certain subunits . Recent data indicate that Polo-related kinases play a role in the activation of the APC/C during mitosis (Charles et al, 1998;Descombes and Nigg, 1998;Shirayama et al, 1998). In S. cerevisiae, the APC/C is activated during the metaphase to anaphase transition and remains active during G1 (Amon et al, 1994), as also occurs in mammalian cells (Brandeis and Hunt, 1996).…”

Section: Introductionmentioning

confidence: 99%

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

Fincher

Tang

et al. 1998

MBoC

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Fincher

Tang

et al. 1998

MBoC

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“…Degradation of Cdc5 in budding yeast is mediated by APC Cdh1 and expression of a nondegradable Cdc5 arrests cells in a G2-like state, lacking mitotic cyclins and a mitotic spindle, suggesting that destruction of this protein is required to inactivate APC-dependent degradation of mitotic cyclins as cells enter S phase (Charles et al, 1998;Shirayama et al, 1998). Accordingly, immunoprecipitation of Plx1 from interphasic Xenopus egg extracts in which APC has been activated by the addition of purified cyclin B/cdk1 induces premature inactivation of cyclin B degradation (Brassac et al, 2000).…”

Section: Apc Substrates Controlling Exit From Mitosismentioning

confidence: 99%

The anaphase-promoting complex: a key factor in the regulation of cell cycle

et al. 2005

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Events controlling cell division are governed by the degradation of different regulatory proteins by the ubiquitin-dependent pathway. In this pathway, the attachment of a polyubiquitin chain to a substrate by an ubiquitin-ligase targets this substrate for degradation by the 26S proteasome. Two different ubiquitin ligases play an important role in the cell cycle: the SCF (Skp1/Cullin/ F-box) and the anaphase-promoting complex (APC). In this review, we describe the present knowledge about the APC. We pay particular attention to the latest results concerning APC structure, APC regulation and substrate recognition, and we discuss the implication of these findings in the understanding the APC function.

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“…The GAL-CDC5-3MYC, and GAL-CDC15 fusions were described in Taylor et al (1997), Charles et al (1998), Visintin et al (1999), and Bardin et al (2003) respectively. The CFI1-GFP and DBF2-3HA fusion were constructed by using the polymerase chain reaction-based method described in Longtine et al (1998).…”

Section: Yeast Strains and Growth Conditionsmentioning

confidence: 99%

The Role of the Polo Kinase Cdc5 in Controlling Cdc14 Localization

Visintin

Stegmeier

Amon

2003

MBoC

119

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In budding yeast, the protein phosphatase Cdc14 controls exit from mitosis. Its activity is regulated by a competitive inhibitor Cfi1/Net1, which binds to and sequesters Cdc14 in the nucleolus. During anaphase, Cdc14 is released from its inhibitor by the action of two regulatory networks. The Cdc Fourteen Early Anaphase Release (FEAR) network initiates Cdc14 release from Cfi1/Net1 during early anaphase, and the Mitotic Exit Network (MEN) promotes Cdc14 release during late anaphase. Here, we investigate the relationship among FEAR network components and propose an order in which they function to promote Cdc14 release from the nucleolus. Furthermore, we examine the role of the protein kinase Cdc5, which is a component of both the FEAR network and the MEN, in Cdc14 release from the nucleolus. We find that overexpression of CDC5 led to Cdc14 release from the nucleolus in S phase-arrested cells, which correlated with the appearance of phosphorylated forms of Cdc14 and Cfi1/Net1. Cdc5 promotes Cdc14 phosphorylation and, by stimulating the MEN, Cfi1/Net1 phosphorylation. Furthermore, we suggest that Cdc14 release from the nucleolus only occurs when Cdc14 and Cfi1/Net1 are both phosphorylated.

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The Polo-related kinase Cdc5 activates and is destroyed by the mitotic cyclin destruction machinery in S. cerevisiae

Abstract: We conclude that Cdc5 is a positive regulator of cyclin-specific APC activity in late mitosis. Degradation of Cdc5 in G1 might provide a feedback mechanism by which the APC destroys its activator at the onset of the next cell cycle.

Cited by 222 publications

References 67 publications

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

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

The anaphase-promoting complex: a key factor in the regulation of cell cycle

The Role of the Polo Kinase Cdc5 in Controlling Cdc14 Localization

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The Polo-related kinase Cdc5 activates and is destroyed by the mitotic cyclin destruction machinery in S. cerevisiae

Abstract: We conclude that Cdc5 is a positive regulator of cyclin-specific APC activity in late mitosis. Degradation of Cdc5 in G1 might provide a feedback mechanism by which the APC destroys its activator at the onset of the next cell cycle.

Cited by 222 publications

References 67 publications

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

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

The anaphase-promoting complex: a key factor in the regulation of cell cycle

The Role of the Polo Kinase Cdc5 in Controlling Cdc14 Localization

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

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