Current Biology
PaperMitotic regulation of protein phosphatases by the fission yeast sds22 protein
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Cited by (107)
The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange
2024, Journal of Biological ChemistryCasein kinase II– dependent phosphorylation of DNA topoisomerase II suppresses the effect of a catalytic topo II inhibitor, ICRF-193, in fission yeast
2019, Journal of Biological ChemistryCitation Excerpt :To increase transfer efficiency, manganese ions were eliminated from the gel by soaking it in transfer buffer containing 1 mm EDTA. Immunoblotting was performed using the following antibodies: anti-FLAG M2 (Sigma), anti-PSTAIR (a gift from Dr. Y. Nagahama, National Institute for Basic Biology, Okazaki, Japan), anti-Cut2 (69), and anti-Cdc13 (70). Top2 phospho-antibodies were obtained by immunizing rabbits with synthetic phosphopeptides (Sigma): (1351-RKTNKPVATTIF[S-phos]SDDEDD-1369) for anti-Top2 phospho-Ser1363 and (1351-RKTNKPVATTIFS[S-phos]DDEDD-1369) for anti-Top2 phospho-Ser1364.
Sds22 participates in Glc7 mediated Rad53 dephosphorylation in MMS-induced DNA damage in Candida albicans
2016, Fungal Genetics and BiologyCitation Excerpt :The LRRs of Sds22 form a curved LRR super-helix fused to a C-terminal LRR-cap that binds to the so-called R4/R5/R6 triangle of Glc7. In fission yeast, Sds22 mutants carrying point mutations in LRR5 or LRR9 or C-terminal truncations failed to enter the nucleus and lost its function (Stone et al., 1993). Two of the residues we mutated in Sds22 are located in the LRR domain with D158 in LRR4 and E202 in LRR6, suggesting that the mutations affect the conformation of the LRR domain leading to reduced affinity to Glc7.
Function of Protein Phosphatase-1, Glc7, in Saccharomyces cerevisiae
2010, Advances in Applied MicrobiologyYPI1 and SDS22 proteins regulate the nuclear localization and function of yeast type 1 phosphatase Glc7
2007, Journal of Biological ChemistryCitation Excerpt :In the latter we found that most of the Sds22, Glc7, and Ypi1 proteins were present in fractions corresponding to an estimated molecular mass of 130 kDa. The existence of this complex would provide an explanation for the isolation in Schizosaccharomyces pombe, by gel filtration, of a trimeric complex of 105 kDa containing Sds22, Sds21 (PP1), and an unidentified phosphoprotein of 25 kDa (23). In this case, the 25-kDa unidentified protein could be the S. pombe orthologue of Ypi1 (GenBank™ accession number CAB11073).
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Present address: Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
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Present address: Department of Biochemistry and Biophysics, University of California School of Medicine, San Francisco, CA 94143, USA.