Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: Self-versus non-self-priming

Lee, Kyung S.; Park, Jung‐Eun; Yong, Kang; Zimmerman, Wendy; Soung, Nak-Kyun; Seong, Yeon-Sun; Kwak, Sahng‐June; Erikson, Raymond L.

doi:10.4161/cc.7.2.5272

Cited by 43 publications

(48 citation statements)

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“…The PLK-dependent, CDKindependent JM resolution and SC breakdown we observe might be due to target recognition by PLK through polo-box-independent or phosphorylation-independent interactions (see Lee et al 2008 for an example) or by polo-box binding to a CDK-independent phosphomark formed by other kinases that are active during meiosis I prophase. Alternatively, PLK recognition of the relevant target might require a CDK-catalyzed phosphorylation, but one that is established earlier in meiosis and that persists in the absence of ongoing CDK activity.…”

Section: Cdc5 Promotes Pachytene Exit Genes and Development 2629mentioning

confidence: 99%

“…Multiple targets for PLK have been identified in animals and budding yeast (Lowery et al 2005;Lee et al 2008), including Ime2 (a meiosis-specific CDK-like kinase), Ndt80 (Supplemental Fig. 3), Mam1 (a monopolin component), and Rec8, the meiosis-specific kleisin subunit of cohesin (Clyne et al 2003;Lee and Amon 2003b).…”

Section: Cdc5 Promotes Pachytene Exit Genes and Development 2629mentioning

confidence: 99%

“…In mammals, PLK substrate recognition often occurs when the polo-box domain binds to a portion of the target that is CDK-phosphorylated (Barr et al 2004;Lowery et al 2005;Lee et al 2008). The PLK-dependent, CDKindependent JM resolution and SC breakdown we observe might be due to target recognition by PLK through polo-box-independent or phosphorylation-independent interactions (see Lee et al 2008 for an example) or by polo-box binding to a CDK-independent phosphomark formed by other kinases that are active during meiosis I prophase.…”

Section: Cdc5 Promotes Pachytene Exit Genes and Development 2629mentioning

confidence: 99%

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Polo-like kinase Cdc5 drives exit from pachytene during budding yeast meiosis

Sourirajan¹,

Lichten²

2008

Genes Dev.

181

299

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In budding yeast, exit from the pachytene stage of meiosis requires the mid-meiosis transcription factor Ndt80, which promotes expression of ∼200 genes. Ndt80 is required for meiotic function of polo-like kinase (PLK, Cdc5) and cyclin-dependent kinase (CDK), two cell cycle kinases previously implicated in pachytene exit. We show that ongoing CDK activity is dispensable for two events that accompany exit from pachytene: crossover formation and synaptonemal complex breakdown. In contrast, CDC5 expression in ndt80⌬ mutants efficiently promotes both events. Thus, Cdc5 is the only member of the Ndt80 transcriptome required for this critical step in meiotic progression. During meiosis, a single round of DNA replication is followed by two successive divisions (meiosis I and meiosis II), producing four haploid gametes. This is achieved by segregation of homologs, homologous chromosomes of different parental origin, during meiosis I, followed by segregation of sister chromatids in meiosis II. During the prophase of meiosis I, progressive chromosome condensation is accompanied by homolog pairing and recombination, which culminate at the pachytene stage, where homologs are paired along their entire lengths and connected by the synaptonemal complex (SC). Upon exit from pachytene, the SC disappears and chromosomes become diffuse, only to recondense at diplotene/diakinesis as visible homologs connected by crossovers.Meiotic recombination initiates in early meiosis I prophase by the formation of DNA double-strand breaks (DSBs), catalyzed by the Spo11 endonuclease (Keeney and Neale 2006). As cells progress toward pachytene, DSBs are repaired to form either noncrossover (NCO) recombinants or joint molecule (JM) intermediates, many of which contain parental homologs connected by double Holliday junctions (Bishop and Zickler 2004). JMs are resolved, primarily as crossover recombinants (COs), at the end of pachytene. Crossovers provide the interhomolog connections that later ensure proper homolog alignment on the metaphase I spindle and thus their accurate segregation at anaphase I.The exit from pachytene is a crucial transition, since it is associated with the resolution of JMs as COs, SC disassembly, and kinetochore modification so that sister kinetochores orient toward the same spindle pole (monoorientation), and the separation of duplicated spindle pole bodies (SPBs), the fungal centrosome equivalents (Shuster and Byers 1989;Xu et al. 1995Xu et al. , 1997Clyne et al. 2003;Lee and Amon 2003b). Failure in any of these processes can result in chromosome nondisjunction and the production of aneuploid progeny. Consequently, checkpoint systems monitor synapsis and recombination and prevent exit from pachytene unless these processes are complete (Roeder and Bailis 2000).Ndt80, a transcription factor first expressed in late pachytene, is a central target of these checkpoint systems (Xu et al. 1995;Tung et al. 2000). Ndt80 activates expression of more than 200 genes at mid-meiosis, including those required for meiotic divisions and spor...

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Section: Cdc5 Promotes Pachytene Exit Genes and Development 2629mentioning

confidence: 99%

Section: Cdc5 Promotes Pachytene Exit Genes and Development 2629mentioning

confidence: 99%

Section: Cdc5 Promotes Pachytene Exit Genes and Development 2629mentioning

confidence: 99%

See 1 more Smart Citation

Polo-like kinase Cdc5 drives exit from pachytene during budding yeast meiosis

Sourirajan¹,

Lichten²

2008

Genes Dev.

181

299

View full text Add to dashboard Cite

show abstract

“…Unlike non-self-priming and binding, which require a priming kinase other than Plk1, this unusual self-promoted mechanism appears to be pivotal for quickly amassing Plk1 at kinetochores and cooperatively regu-lating Plk1-dependent biochemical processes at these sites (11)(12)(13). Ironically, however, the level of PBIP1 at late interphase and early mitotic kinetochores diminishes precipitously as an increasing amount of Plk1 is recruited to these sites (10).…”

mentioning

confidence: 99%

“…It has been demonstrated that Plk1 localization to late interphase and early mitotic kinetochores is regulated primarily by the ability of Plk1 itself to phosphorylate the Thr-78 motif of a kinetochore scaffold protein, PBIP1 (also called MLF1IP and CENP-U/50), and bind to it (10) through a mechanism called self-priming and binding (11,12). Unlike non-self-priming and binding, which require a priming kinase other than Plk1, this unusual self-promoted mechanism appears to be pivotal for quickly amassing Plk1 at kinetochores and cooperatively regu-lating Plk1-dependent biochemical processes at these sites (11)(12)(13).…”

mentioning

confidence: 99%

Mammalian Polo-like Kinase 1 (Plk1) Promotes Proper Chromosome Segregation by Phosphorylating and Delocalizing the PBIP1·CENP-Q Complex from Kinetochores

Park

Kim

et al. 2015

Journal of Biological Chemistry

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Background: Plk1 is a protein kinase that localizes to subcellular structures called kinetochores to promote mitotic progression. Results: Plk1 interacts with and regulates a kinetochore-associated PBIP1⅐CENP-Q complex. Conclusion: This is a tightly regulated, cell cycle-dependent process, the deregulation of which leads to improper chromosome segregation and mitotic progression. Significance: This event is likely critical for maintaining genomic integrity and preventing aneuploidy.

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Polo-box domain: a versatile mediator of polo-like kinase function

Park

Soung

Johmura

et al. 2010

Cell. Mol. Life Sci.

Self Cite

144

154

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Members of the polo subfamily of protein kinases have emerged as important regulators in diverse aspects of the cell cycle and cell proliferation. A large body of evidence suggests that a highly conserved polo-box domain (PBD) present in the C-terminal non-catalytic region of polo kinases play a pivotal role in the function of these enzymes. Recent advances in our comprehension of the mechanisms underlying mammalian polo-like kinase 1 (Plk1)-dependent protein-protein interactions revealed that the PBD serves as an essential molecular mediator that brings the kinase domain of Plk1 in proximity with its substrates mainly through phospho-dependent interactions with its target proteins. In this review, current understanding of the structure and functions of PBD, mode of PBDdependent interactions and substrate phosphorylation, and other phospho-independent functions of PBD are discussed.

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Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: Self-versus non-self-priming

Cited by 43 publications

References 0 publications

Polo-like kinase Cdc5 drives exit from pachytene during budding yeast meiosis

Polo-like kinase Cdc5 drives exit from pachytene during budding yeast meiosis

Mammalian Polo-like Kinase 1 (Plk1) Promotes Proper Chromosome Segregation by Phosphorylating and Delocalizing the PBIP1·CENP-Q Complex from Kinetochores

Polo-box domain: a versatile mediator of polo-like kinase function

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