Temporal and spatial expression patterns of Cdc25 phosphatase isoforms during early Xenopus development

Nakajo, Nobushige; Deno, Yu ki; Ueno, Hiroyuki; Kenmochi, Chihiro; Shimuta, Ken; Sagata, Noriyuki

doi:10.1387/ijdb.113287nn

Cited by 8 publications

(10 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Four Cdc25 family phosphatases (Cdc25A, Cdc25B, Cdc25C and Cdc25D) have been identified in Xenopus . Among these, only Cdc25C is present in oocytes and eggs, and acts as the physiological M‐phase inducer in egg extracts.…”

Section: Resultsmentioning

confidence: 99%

“…Oocyte maturation-promoting activities of Xenopus Cdc25A and Cdc25C were differently regulated by N-terminal truncations Four Cdc25 family phosphatases (Cdc25A, Cdc25B, Cdc25C and Cdc25D) have been identified in Xenopus [32,33]. Among these, only Cdc25C is present in oocytes and eggs, and acts as the physiological Mphase inducer in egg extracts.…”

Section: Xenopus Cdc25c Was Converted Into Smaller Fragments In Apoptmentioning

confidence: 99%

See 1 more Smart Citation

Dual inhibition of Cdc2 protein kinase activation during apoptosis in Xenopus egg extracts

2015

View full text Add to dashboard Cite

When intracellular damage accumulates in proliferating somatic cells, the cell cycle usually arrests in G 1 or G 2 in a checkpoint-dependent manner, either to repair the damage or to die by apoptosis. In contrast, early embryonic cells lack checkpoint-mediated cell-cycle arrest, and it is not clear whether apoptosis in early embryonic cells occurs at a specific cell cycle stage or at random points. Here, we examined the functional molecular link between the embryonic cell cycle and apoptosis using Xenopus egg extracts. When apoptosis was induced in egg extracts by addition of exogenous cytochrome c during cellcycle progression, cyclin B accumulation was inhibited, Cdc2 was not activated, and the cell cycle arrested at interphase. However, addition of recombinant cyclin B failed to activate Cdc2 due to the strong inhibitory phosphorylation of Cdc2 Tyr15 in apoptotic egg extracts. We found that endogenous Cdc25C, which activates the Cdc2-cyclin B complex by dephosphorylating Cdc2 Tyr15, was inactivated by caspase-mediated cleavage at two sites in the N-terminal regulatory domain. When the hyperactive Cdc25A catalytic fragment was added together with recombinant cyclin B to artificially dephosphorylate Cdc2 Tyr15, M-phase induction was restored in apoptotic egg extracts, indicating that the blockage of cyclin B accumulation and the caspase-mediated inactivation of Cdc25C dually inhibited Cdc2 activation. Apoptosis induction in cytostatic factor-arrested metaphase egg extracts resulted in inactivation of Cdc2 without cyclin B degradation. These results suggest that apoptotic inactivation of Cdc25C plays an important role in arresting the embryonic cell cycle at interphase during apoptosis.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Xenopus Cdc25c Was Converted Into Smaller Fragments In Apoptmentioning

confidence: 99%

Dual inhibition of Cdc2 protein kinase activation during apoptosis in Xenopus egg extracts

2015

View full text Add to dashboard Cite

show abstract

“…Protein phosphatase is divided into serine/threonine phosphatases, tyrosine phosphatase and DSP. DSP has both the functions of serine/threonine phosphatases phosphorylating serine/threonine and tyrosine phosphatase to dephosphorylate tyrosine (Lavecchia (Lew and Kornbluth, 1996;Sanchez et al, 1997;Folch-Mallol et al, 2004;Nakajo et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Cloning and Expression Analysis of Cdc25 Gene of <i>Sipunculus nudus</i> in Oocytes

Su¹,

Ye²,

Liu³

et al. 2020

ijms

View full text Add to dashboard Cite

Cell division cycle 25 ( Cdc25) is an important dual specificity phosphatase, which plays an important role in regulating the process of oocytes meiosis and embryo development. In our study, the full-length cDNA of Cdc25 from S. nudus (Sn-Cdc25) was cloned by using RACE technology. The results show that Sn-Cdc25 is 4 130 bp in length, including 3' UTR 1 849 bp and 5' UTR 427 bp. The Open reading frame (ORF) is 1 854 bp which encodes 617 amino acids. Sequence analysis shows that the molecular weight of Sn-Cdc25 protein is 69.58 kD, with two typical Cdc25 protein domains: M-phase inducer phosphatase domain, Rhodanese-like domain, and the active site sequence HCX5R which can catalyze the dephosphorylation process. Multi-sequence alignment finds that the C-terminal homology is higher than the N-terminal. The tertiary structure prediction shows that the spatial conformation of Cdc25 homologous protein and their active site is highly conservative. The total of 5 Motifs are found in Motif analysis, of which Motif 1 and Motif 2 are Paxillin LD motif and MYND domain binding motif, respectively. Phylogenetic tree analysis shows that Cdc25 is clustered into two branches: invertebrate and vertebrate. qRT-PCR results show that the expression of Sn-Cdc25, with two peaks, is significantly different in different developmental stages of oocytes. The increased expression of Sn-Cdc25 may be related to the process of Cdc25 promoting DNA replication from the the early stage of yolk formation to the late stage of vigorous yolk synthesis (O1-O3). When the oocytes entering metanephridium from coelomic fluid, the rapid rise of Sn-Cdc25 expression may be beneficial to the activation of maturation promoting factor (MPF). The above results have accumulated basic data for further understanding of the developmental mechanism of Sipuncula oocytes and the optimization of artificial breeding techniques.

show abstract

“…The evolution of the Cdc25 homologs identified in the animals (Cdc25A, Cdc25B and Cdc25C) shows a high degree of similarity among various methods. Cdc25D proteins identified in zebrafish and Xenopus show the greatest similarity to each other, rather than to any of Cdc25A, Cdc25B or Cdc25C [53], but, however, they rarely occur on the same branch. It can be concluded that the common ancestor of Cdc25A and Cdc25B proteins has been separated from other animal Cdc25 homologs first.…”

Section: Relationships Of Cdc25-like Proteinsmentioning

confidence: 92%

Phylogenetic Analyses of Proteins Coordinating G2 Size Control in Fission Yeast

Nagy¹,

Medgyes-Horváth²,

Szalay³

et al. 2019

Period. Polytech. Chem. Eng.

View full text Add to dashboard Cite

Regulation of G2 phase is based on inhibition of MPF (M-phase Promoting Factor) through phosphorylation by Wee1-like kinases. Removal of the inhibiting phosphate group requires Cdc25-like phosphatases. In fission yeast, size control is achieved by monitoring cell length via interactions of Pom1, Nif1, Cdr1 and Cdr2 proteins, regulating MPF via the Wee1 kinase. Here, a search for homologues of these key proteins was performed in the genomes of several model organisms to analyze the evolution of G2 size control. Both the known upstream pathways regulating Wee1 protein (Pom1 → Cdr2, and Nif1 → Cdr1) have been found to be characteristic only in fission yeasts. Mik1, a backup copy of Wee1 kinase probably appeared in the common ancestor of the fission yeasts. The duplication resulting in Wee1A and Wee1B isoforms probably happened in a common ancestor of higher animals, while the Myt1 protein (found only in animals) could be a variant between an ancient serine / threonine kinase and the Wee1 tyrosine kinase. Probably both the ancestors of plants and that of fungi may have lost the myt1 gene. In fission yeasts, Pyp3 is a backup phosphatase of Cdc25, also activating MPF in late G2. Interestingly, we found that the small Ibp1 phosphatase appeared to be a closer homologue of Cdc25, although its function is different. Moreover, Cdc25 homologues identified in plants were found to be more closely related to Ibp1 rather than to Cdc25 of fission yeast. In the Cdc25-like proteins, a novel conserved region was found with the consensus sequence LxxG(Y/F).

show abstract

Temporal and spatial expression patterns of Cdc25 phosphatase isoforms during early Xenopus development

Cited by 8 publications

References 17 publications

Dual inhibition of Cdc2 protein kinase activation during apoptosis in Xenopus egg extracts

Dual inhibition of Cdc2 protein kinase activation during apoptosis in Xenopus egg extracts

Cloning and Expression Analysis of Cdc25 Gene of <i>Sipunculus nudus</i> in Oocytes

Phylogenetic Analyses of Proteins Coordinating G2 Size Control in Fission Yeast

Contact Info

Product

Resources

About