Activator of mitotic machinery Cdc14 phosphatase activation C-term
SMART accession number:
SM01327
Description:
This region of the Zds1 protein is critical for sporulation and has also been shown to suppress the calcium sensitivity of Zds1 deletions (PMID:16322512). The C-terminal motif is common to both Zds1 and Zds2 proteins, both of which are putative interactors of Cdc55 and are required for the completion of mitotic exit and cytokinesis. They both contribute to timely Cdc14 activation during mitotic exit and are required downstream of separase to facilitate nucleolar Cdc14 (PMID:18762578).
This region of the Zds1 protein is critical for sporulation and has also been shown to suppress the calcium sensitivity of Zds1 deletions [ (PUBMED:16322512) ]. The C-terminal motif is common to both Zds1 and Zds2 proteins, both of which are putative interactors of Cdc55 and are required for the completion of mitotic exit and cytokinesis. They both contribute to timely Cdc14 activation during mitotic exit and are required downstream of separase to facilitate nucleolar Cdc14 release[ (PUBMED:18762578) ].
Family alignment:
There are 583 Zds_C domains in 582 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Zds_C domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Zds_C domain is also avaliable.
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Separase cooperates with Zds1 and Zds2 to activate Cdc14 phosphatase in earlyanaphase.
J Cell Biol. 2008; 182: 873-83
Display abstract
Completion of mitotic exit and cytokinesis requires the inactivation of mitoticcyclin-dependent kinase (Cdk) activity. A key enzyme that counteracts Cdk during budding yeast mitotic exit is the Cdc14 phosphatase. Cdc14 is inactive for muchof the cell cycle, sequestered by its inhibitor Net1 in the nucleolus. Atanaphase onset, separase-dependent down-regulation of PP2A(Cdc55) allowsphosphorylation of Net1 and consequent Cdc14 release. How separase causesPP2A(Cdc55) down-regulation is not known. Here, we show that twoCdc55-interacting proteins, Zds1 and Zds2, contribute to timely Cdc14 activation during mitotic exit. Zds1 and Zds2 are required downstream of separase tofacilitate nucleolar Cdc14 release. Ectopic Zds1 expression in turn is sufficientto down-regulate PP2A(Cdc55) and promote Net1 phosphorylation. These findingsidentify Zds1 and Zds2 as new components of the mitotic exit machinery, involved in activation of the Cdc14 phosphatase at anaphase onset. Our results suggestthat these proteins may act as separase-regulated PP2A(Cdc55) inhibitors.
zds1, a novel gene encoding an ortholog of Zds1 and Zds2, controls sexualdifferentiation, cell wall integrity and cell morphology in fission yeast.
Genetics. 2006; 172: 811-25
Display abstract
While screening for genes that reverse the sporulation-deficient phenotype of theras1delta diploid Schizosaccharomyces pombe strain, we identified zds1. This geneshares sequence homology with the ZDS1 and ZDS2 genes from Saccharomycescerevisiae, which appear to be involved in multiple cellular events. Expressionof Zds1 in ras1delta diploid cells elevated their sporulation rate from 0.3 to11.2%. Expression of the Zds1 C-terminal region increased the sporulation ratefurther (to 21.9%) while introduction of the Zds1 N-terminal region had noeffect. zds1 expression did not induce sporulation in strains with mutations ingenes participating in the downstream MAP kinase cascade. The zds1-disruptedstrain is sensitive to CaCl2, and this effect is suppressed by the C-terminalregion of Zds1. The growth of the zds1delta strain is markedly inhibited by cold temperatures, while its viability decreased in the stationary phase. Moreover,the zds1delta strain is round in shape and very sensitive to zymolyase, and itscell wall becomes thicker than that of wild type. Thus, zds1 must be required to maintain cell wall integrity. The Zds1-GFP fusion protein localized to thecytosol, the septum, and the cell cortex. Its localization in the septum wasdependent on its C-terminal region. Overexpression of the C-terminal region ofZds1 induced multi-septa and abnormal zygotes. We propose that the C-terminalregion is the functional domain of Zds1 while the N-terminal region is a negativeregulatory region. Thus, Zds1 is involved in multiple cellular events in fission yeast, including sexual differentiation, Ca2+ tolerance, cell wall integrity,viability in the stationary phase, and cell morphology.
Links (links to other resources describing this domain)
