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Chemogenetic profiling reveals PP2A‐independent cytotoxicity of proposed PP2A activators iHAP1 and DT‐061

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Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit

Holder, J. W., Mohammed, S., & Barr, F. A. (2020) · eLife · doi:10.7554/elife.59885 · Cited by 33 · see citing works

PPP2R2A prostate cancer haploinsufficiency is associated with worse prognosis and a high vulnerability to B55α/PP2A reconstitution that triggers centrosome destabilization

Zhao, Z., Kurimchak, A., Nikonova, A. S., Feiser, F., Wasserman, J. S., Fowle, H. A., Varughese, T., Connors, M., Johnson, K. J., Makhov, P. B., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0180-9 · Cited by 31 · see citing works

Emerging insights into serine/threonine-specific phosphoprotein phosphatase function and selectivity

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Cyclin A and Cks1 promote kinase consensus switching to non-proline-directed CDK1 phosphorylation

al-Rawi, A., Kaye, E., Korolchuk, S., Endicott, J., & Ly, T. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112139 · Cited by 27 · see citing works

The Role of Phosphatases in Nuclear Envelope Disassembly and Reassembly and Their Relevance to Pathologies

Huguet, F., Flynn, S., & Vagnarelli, P. (2019) · Cells · doi:10.3390/cells8070687 · Cited by 30 · see citing works

Quantitative kinase and phosphatase profiling reveal that CDK1 phosphorylates PP2Ac to promote mitotic entry

Nasa, I., Cressey, L. E., Kruse, T., Hertz, E. P. T., Gui, J., Graves, L. M., Nilsson, J., & Kettenbach, A. N. (2020) · Science Signaling · doi:10.1126/scisignal.aba7823 · Cited by 28 · see citing works

Coupling TOR to the Cell Cycle by the Greatwall–Endosulfine–PP2A-B55 Pathway

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The dNTP triphosphohydrolase activity of SAMHD1 persists during S-phase when the enzyme is phosphorylated at T592

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A signal capture and proofreading mechanism for the KDEL-receptor explains selectivity and dynamic range in ER retrieval

Gerondopoulos, A., Bräuer, P., Sobajima, T., Wu, Z., Parker, J. L., Biggin, P. C., Barr, F. A., & Newstead, S. L. (2021) · eLife · doi:10.7554/elife.68380 · Cited by 29 · see citing works

SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast

Baró, B., Játiva, S., Calabria, I., Vinaixa, J., Bech‐Serra, J. J., de LaTorre, C., Rodrigues, J., Hernáez, M. L., Gil, C., Barceló-Batllori, S., et al. (2018) · GigaScience · doi:10.1093/gigascience/giy047 · Cited by 28 · see citing works

Mechanisms of signalling-memory governing progression through the eukaryotic cell cycle

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Regulation of PP2A, PP4, and PP6 holoenzyme assembly by carboxyl-terminal methylation

Lyons, S. P., Greiner, E. C., Cressey, L. E., Adamo, M. E., & Kettenbach, A. N. (2021) · Scientific Reports · doi:10.1038/s41598-021-02456-z · Cited by 27 · see citing works

Substrate recognition principles for the PP2A-B55 protein phosphatase

Kruse, T., Garvanska, D. H., Varga, J. K., Garland, W., McEwan, B. C., Hein, J. B., Weisser, M. B., Benavides-Puy, I., Chan, C. B., Sotelo-Parrilla, P., et al. (2024) · Science Advances · doi:10.1126/sciadv.adp5491 · Cited by 26 · see citing works

The Cell Cycle Checkpoint System MAST(L)-ENSA/ARPP19-PP2A is Targeted by cAMP/PKA and cGMP/PKG in Anucleate Human Platelets

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PP2A‐B56 binds to Apc1 and promotes Cdc20 association with the APC/C ubiquitin ligase in mitosis

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Interlinked bistable mechanisms generate robust mitotic transitions

Hutter, L. H., Rata, S., Hochegger, H., & Novák, B. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1371885 · Cited by 25 · see citing works

PP1 promotes cyclin B destruction and the metaphase–anaphase transition by dephosphorylating CDC20

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Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes

Swartz, S. Z., Nguyen, H. T., McEwan, B. C., Adamo, M. E., Cheeseman, I. M., & Kettenbach, A. N. (2021) · eLife · doi:10.7554/elife.70588 · Cited by 24 · see citing works

A mitotic CDK5-PP4 phospho-signaling cascade primes 53BP1 for DNA repair in G1

Zheng, X.-F., Acharya, S. S., Choe, K. N., Nikhil, K., Adelmant, G., Satapathy, S. R., Sharma, S., Viccaro, K., Rana, S., Natarajan, A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12084-x · Cited by 24 · see citing works

Protein interactomes of protein phosphatase 2A B55 regulatory subunits reveal B55-mediated regulation of replication protein A under replication stress

Wang, F., Zhu, S., Fisher, L. A., Wang, W., Oakley, G. G., Li, C., & Peng, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-21040-6 · Cited by 23 · see citing works

Novel perspectives of target-binding by the evolutionarily conserved PP4 phosphatase

Kármán, Z., Réthi‐Nagy, Z., Ábrahám, E., Fabri-Ordogh, L., Csonka, Á., Vilmos, P., Dȩbski, J., Dadlez, M., Glover, D. M., & Lipinszki, Z. (2020) · Open Biology · doi:10.1098/rsob.200343 · Cited by 22 · see citing works

Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A Recruitment

Sonntag, T., Ostojić, J., Vaughan, J. M., Moresco, J. J., Yoon, Y., Yates, J. R., & Montminy, M. (2018) · iScience · doi:10.1016/j.isci.2018.12.012 · Cited by 22 · see citing works

Back to the new beginning: Mitotic exit in space and time

Vagnarelli, P. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.03.010 · Cited by 20 · see citing works

Dephosphorylation in nuclear reassembly after mitosis

Archambault, V., Li, J., Emond-Fraser, V., & Larouche, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1012768 · Cited by 21 · see citing works

Phosphatase specificity principles uncovered by MRBLE:Dephos and global substrate identification

Hein, J. B., Nguyen, H. T., Garvanska, D. H., Nasa, I., Kruse, T., Feng, Y., Mendez, B. L., Davey, N. E., Kettenbach, A. N., Fordyce, P. M., et al. (2023) · Molecular Systems Biology · doi:10.15252/msb.202311782 · Cited by 20 · see citing works

Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis

Kataria, M., & Yamano, H. (2019) · Cells · doi:10.3390/cells8080814 · Cited by 21 · see citing works

Greatwall-Endosulfine: A Molecular Switch that Regulates PP2A/B55 Protein Phosphatase Activity in Dividing and Quiescent Cells

García-Blanco, N., Vázquez-Bolado, A., & Moreno, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20246228 · Cited by 21 · see citing works

A PP2A-B56—Centered View on Metaphase-to-Anaphase Transition in Mouse Oocyte Meiosis I

Keating, L., Touati, S. A., & Wassmann, K. (2020) · Cells · doi:10.3390/cells9020390 · Cited by 21 · see citing works

Effects of carboxyl-terminal methylation on holoenzyme function of the PP2A subfamily

Nasa, I., & Kettenbach, A. N. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200177 · Cited by 21 · see citing works

Protein phosphatase 2A regulatory subunit B55α functions in mouse oocyte maturation and early embryonic development

Liang, S., Guo, J., Choi, J.-W., Shin, K.-T., Wang, H.-Y., Jo, Y.-J., Kim, N.-H., & Cui, X.-S. (2017) · Oncotarget · doi:10.18632/oncotarget.15927 · Cited by 20 · see citing works

The Greatwall kinase safeguards the genome integrity by affecting the kinome activity in mitosis

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Structural, enzymatic and spatiotemporal regulation of PP2A-B55 phosphatase in the control of mitosis

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Protein phosphatase 2A in the healthy and failing heart: New insights and therapeutic opportunities

Sergienko, N. M., Donner, D. G., Delbridge, L. M. D., McMullen, J. R., & Weeks, K. L. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110213 · Cited by 19 · see citing works

The M-phase regulatory phosphatase PP2A-B55δ opposes protein kinase A on Arpp19 to initiate meiotic division

Lemonnier, T., Daldello, E. M., Poulhe, R., Le, T., Miot, M., Lignières, L., Jessus, C., & Dupré, A. (2021) · Nature Communications · doi:10.1038/s41467-021-22124-0 · Cited by 18 · see citing works

The study of the determinants controlling Arpp19 phosphatase-inhibitory activity reveals an Arpp19/PP2A-B55 feedback loop

Labbé, J. C., Vigneron, S., Méchali, F., Robert, P., Roque, S., Genoud, C., Goguet-Rubio, P., Barthe, P., Labesse, G., Cohen‐Gonsaud, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23657-0 · Cited by 17 · see citing works

AMPK regulates anaphase central spindle length by phosphorylation of KIF4A

Li, Q., Yan, X., Guo, L., Li, J. X., & Zang, Y. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx029 · Cited by 17 · see citing works

Coupling of Cdc20 inhibition and activation by BubR1

Hein, J. B., Garvanska, D. H., Nasa, I., Kettenbach, A. N., & Nilsson, J. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202012081 · Cited by 17 · see citing works

A phosphatase-centric mechanism drives stress signaling response

Hollenstein, D. M., Gérecová, G., Romanov, N., Ferrari, J., Veis, J., Janschitz, M., Beyer, R., Schüller, C., Ogris, E., Hartl, M., et al. (2021) · EMBO Reports · doi:10.15252/embr.202152476 · Cited by 17 · see citing works

PP2A Functions during Mitosis and Cytokinesis in Yeasts

Moyano-Rodríguez, Y., & Queralt, E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010264 · Cited by 16 · see citing works

PP2A-B55γ counteracts Cdk1 and regulates proper spindle orientation through the cortical dynein adaptor NuMA

Keshri, R., Rajeevan, A., & Kotak, S. (2020) · Journal of Cell Science · doi:10.1242/jcs.243857 · Cited by 16 · see citing works

Quantitative phosphoproteomics to unravel the cellular response to chemical stressors with different modes of action

Sampadi, B. K., Pines, A., Munk, S., Mišovic, B., de Groot, A. J. L., van de Water, B., Olsen, J. V., Mullenders, L. H. F., & Vrieling, H. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02712-7 · Cited by 14 · see citing works

DUSP3 maintains genomic stability and cell proliferation by modulating NER pathway and cell cycle regulatory proteins

Russo, L. C., Farias, J. O., & Forti, F. L. (2020) · Cell Cycle · doi:10.1080/15384101.2020.1762043 · Cited by 15 · see citing works

Regulation of minimal spindle midzone organization by mitotic kinases

Lim, W. M., Chew, W.-X., Esposito-Verza, A., Pesenti, M. E., Musacchio, A., & Surrey, T. (2024) · Nature Communications · doi:10.1038/s41467-024-53500-1 · Cited by 15 · see citing works

Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions

Hoermann, B., & Köhn, M. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200175 · Cited by 14 · see citing works

Identification of PP2A-B55 targets uncovers regulation of emerin during nuclear envelope reassembly in Drosophila

Emond-Fraser, V., Larouche, M., Kubiniok, P., Bonneil, É., Li, J., Bourouh, M., Frizzi, L., Thibault, P., & Archambault, V. (2023) · Open Biology · doi:10.1098/rsob.230104 · Cited by 14 · see citing works

Gradual compaction of the central spindle decreases its dynamicity in PRC1 and EB1 gene-edited cells

Asthana, J., Cade, N. I., Normanno, D., Lim, W. M., & Surrey, T. (2021) · Life Science Alliance · doi:10.26508/lsa.202101222 · Cited by 14 · see citing works

Protein phosphatase 2A catalytic subunit β suppresses PMA/ionomycin‐induced T‐cell activation by negatively regulating PI3K/Akt signaling

Gao, R., Li, X., Gao, H., Zhao, K., Liu, X., Liu, J., Wang, Q., Zhu, Y., Chen, H., Xiang, S., et al. (2022) · FEBS Journal · doi:10.1111/febs.16370 · Cited by 14 · see citing works

Express yourself: how PP2A-B55Pab1 helps TORC1 talk to TORC2

Martín, R., & López‐Avilés, S. (2017) · Current Genetics · doi:10.1007/s00294-017-0721-8 · Cited by 14 · see citing works

Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A–Cdc55 at anaphase onset

Játiva, S., Calabria, I., Moyano-Rodríguez, Y., Garcia, P. S., & Queralt, E. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03086-5 · Cited by 14 · see citing works

BUB-1-bound PLK-1 directs CDC-20 kinetochore recruitment to ensure timely embryonic mitoses

Houston, J., Ohta, M., Gómez-Cavazos, J. S., Deep, A., Corbett, K. D., Oegema, K., Lara-Gonzalez, P., Kim, T., & Desai, A. (2023) · Current Biology · doi:10.1016/j.cub.2023.04.021 · Cited by 13 · see citing works

Kinetochore Recruitment of the Spindle and Kinetochore-Associated (Ska) Complex Is Regulated by Centrosomal PP2A in Caenorhabditis elegans

Lange, K. I., Suleman, A., & Srayko, M. (2019) · Genetics · doi:10.1534/genetics.119.302105 · Cited by 12 · see citing works

Protein phosphatases at the nuclear envelope

Gil, R. S., de Castro, I. J., Berihun, J., & Vagnarelli, P. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170139 · Cited by 11 · see citing works

Mitotic exit: Determining the PP2A dephosphorylation program

Pereira, G., & Schiebel, E. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201608019 · Cited by 6 · see citing works

Global substrate identification and high throughput in vitro dephosphorylation reactions uncover PP1 and PP2A-B55 specificity principlesPreprint

Hein, J. B., Nguyen, H. T., Garvanska, D. H., Nasa, I., Feng, Y., Mendez, B. L., Davey, N. E., Kettenbach, A. N., Fordyce, P. M., & Nilsson, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.14.540683 · Cited by 2 · see citing works

Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation

Kamenz, J. L., Gelens, L., & Ferrell, J. E. (2020) · Current Biology · doi:10.1016/j.cub.2020.11.058 · Cited by 39 · see citing works

Regulated activity of PP2A–B55δ is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts

Mochida, S., Ikeo, S., Gannon, J., & Hunt, T. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.238 · Cited by 276 · see citing works

Phosphatase specificity principles uncovered by MRBLE:Dephos and global substrate identification

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