Wieser, S. & Pines, J. The biochemistry of mitosis. Cold Spring Harb. Perspect. Biol. 7, a015776 (2015).
Dhavan, R. & Tsai, L. H. A decade of CDK5. Nat. Rev. Mol. Cell Biol. 2, 749â759 (2001).
Malumbres, M. Cyclin-dependent kinases. Genome Biol. 15, 122 (2014).
Coverley, D., Laman, H. & Laskey, R. A. Distinct roles for cyclins E and A during DNA replication complex assembly and activation. Nat. Cell Biol. 4, 523â528 (2002).
Desai, D., Wessling, H. C., Fisher, R. P. & Morgan, D. O. Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2. Mol. Cell. Biol. 15, 345â350 (1995).
Brown, N. R. et al. CDK1 structures reveal conserved and unique features of the essential cell cycle CDK. Nat. Commun. 6, 6769 (2015).
Strauss, B. et al. Cyclin B1 is essential for mitosis in mouse embryos, and its nuclear export sets the time for mitosis. J. Cell Biol. 217, 179â193 (2018).
Gavet, O. & Pines, J. Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis. J. Cell Biol. 189, 247â259 (2010).
Barbiero, M. et al. Cell cycle-dependent binding between cyclin B1 and Cdk1 revealed by time-resolved fluorescence correlation spectroscopy. Open Biol. 12, 220057 (2022).
Pines, J. & Hunter, T. Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2. Cell 58, 833â846 (1989).
Clute, P. & Pines, J. Temporal and spatial control of cyclin B1 destruction in metaphase. Nat. Cell Biol. 1, 82â87 (1999).
Potapova, T. A. et al. The reversibility of mitotic exit in vertebrate cells. Nature 440, 954â958 (2006).
Basu, S., Greenwood, J., Jones, A. W. & Nurse, P. Core control principles of the eukaryotic cell cycle. Nature 607, 381â386 (2022).
Santamaria, D. et al. Cdk1 is sufficient to drive the mammalian cell cycle. Nature 448, 811â815 (2007).
Zheng, X. F. et al. A mitotic CDK5-PP4 phospho-signaling cascade primes 53BP1 for DNA repair in G1. Nat. Commun. 10, 4252 (2019).
Fagerberg, L. et al. Analysis of the human tissue-specific expression by genome-wide integration of transcriptomics and antibody-based proteomics. Mol. Cell. Proteom. 13, 397â406 (2014).
Pozo, K. & Bibb, J. A. The emerging role of Cdk5 in cancer. Trends Cancer 2, 606â618 (2016).
Sharma, S. & Sicinski, P. A kinase of many talents: non-neuronal functions of CDK5 in development and disease. Open Biol. 10, 190287 (2020).
Sun, K. H. et al. Novel genetic tools reveal Cdk5âs major role in Golgi fragmentation in Alzheimerâs disease. Mol. Biol. Cell 19, 3052â3069 (2008).
Sharma, S. et al. Targeting the cyclin-dependent kinase 5 in metastatic melanoma. Proc. Natl Acad. Sci. USA 117, 8001â8012 (2020).
Nabet, B. et al. The dTAG system for immediate and target-specific protein degradation. Nat. Chem. Biol. 14, 431â441 (2018).
Simpson, L. M. et al. Target protein localization and its impact on PROTAC-mediated degradation. Cell Chem. Biol. 29, 1482â1504 e1487 (2022).
Vassilev, L. T. et al. Selective small-molecule inhibitor reveals critical mitotic functions of human CDK1. Proc. Natl Acad. Sci. USA 103, 10660â10665 (2006).
Janssen, A. F. J., Breusegem, S. Y. & Larrieu, D. Current methods and pipelines for image-based quantitation of nuclear shape and nuclear envelope abnormalities. Cells 11, 347 (2022).
Thompson, S. L. & Compton, D. A. Chromosome missegregation in human cells arises through specific types of kinetochore-microtubule attachment errors. Proc. Natl Acad. Sci. USA 108, 17974â17978 (2011).
Kline-Smith, S. L. & Walczak, C. E. Mitotic spindle assembly and chromosome segregation: refocusing on microtubule dynamics. Mol. Cell 15, 317â327 (2004).
Prosser, S. L. & Pelletier, L. Mitotic spindle assembly in animal cells: a fine balancing act. Nat. Rev. Mol. Cell Biol. 18, 187â201 (2017).
Zeng, X. et al. Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage. Cancer Cell 18, 382â395 (2010).
Warren, J. D., Orr, B. & Compton, D. A. A comparative analysis of methods to measure kinetochore-microtubule attachment stability. Methods Cell. Biol. 158, 91â116 (2020).
Gregan, J., Polakova, S., Zhang, L., Tolic-Norrelykke, I. M. & Cimini, D. Merotelic kinetochore attachment: causes and effects. Trends Cell Biol 21, 374â381 (2011).
Etemad, B., Kuijt, T. E. & Kops, G. J. Kinetochore-microtubule attachment is sufficient to satisfy the human spindle assembly checkpoint. Nat. Commun. 6, 8987 (2015).
Tauchman, E. C., Boehm, F. J. & DeLuca, J. G. Stable kinetochore-microtubule attachment is sufficient to silence the spindle assembly checkpoint in human cells. Nat. Commun. 6, 10036 (2015).
Mitchison, T. & Kirschner, M. Microtubule assembly nucleated by isolated centrosomes. Nature 312, 232â237 (1984).
Fourest-Lieuvin, A. et al. Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-dependent kinase Cdk1. Mol. Biol. Cell 17, 1041â1050 (2006).
Ubersax, J. A. et al. Targets of the cyclin-dependent kinase Cdk1. Nature 425, 859â864 (2003).
Yang, C. H., Lambie, E. J. & Snyder, M. NuMA: an unusually long coiled-coil related protein in the mammalian nucleus. J. Cell Biol. 116, 1303â1317 (1992).
Yang, C. H. & Snyder, M. The nuclear-mitotic apparatus protein is important in the establishment and maintenance of the bipolar mitotic spindle apparatus. Mol. Biol. Cell 3, 1259â1267 (1992).
Kotak, S., Busso, C. & Gonczy, P. NuMA phosphorylation by CDK1 couples mitotic progression with cortical dynein function. EMBO J. 32, 2517â2529 (2013).
Kitagawa, M. et al. Cdk1 coordinates timely activation of MKlp2 kinesin with relocation of the chromosome passenger complex for cytokinesis. Cell Rep. 7, 166â179 (2014).
Schrock, M. S. et al. MKLP2 functions in early mitosis to ensure proper chromosome congression. J. Cell Sci. 135, jcs259560 (2022).
Sun, M. et al. NuMA regulates mitotic spindle assembly, structural dynamics and function via phase separation. Nat. Commun. 12, 7157 (2021).
Chen, Q., Zhang, X., Jiang, Q., Clarke, P. R. & Zhang, C. Cyclin B1 is localized to unattached kinetochores and contributes to efficient microtubule attachment and proper chromosome alignment during mitosis. Cell Res. 18, 268â280 (2008).
Kabeche, L. & Compton, D. A. Cyclin A regulates kinetochore microtubules to promote faithful chromosome segregation. Nature 502, 110â113 (2013).
Hegarat, N. et al. Cyclin A triggers mitosis either via the Greatwall kinase pathway or cyclin B. EMBO J. 39, e104419 (2020).
Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583â589 (2021).
Wood, D. J. & Endicott, J. A. Structural insights into the functional diversity of the CDK-cyclin family. Open Biol. 8, 180112 (2018).
Brown, N. R., Noble, M. E., Endicott, J. A. & Johnson, L. N. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell Biol. 1, 438â443 (1999).
Tarricone, C. et al. Structure and regulation of the CDK5-p25nck5a complex. Mol. Cell 8, 657â669 (2001).
Poon, R. Y., Lew, J. & Hunter, T. Identification of functional domains in the neuronal Cdk5 activator protein. J. Biol. Chem. 272, 5703â5708 (1997).
Oppermann, F. S. et al. Large-scale proteomics analysis of the human kinome. Mol. Cell. Proteom. 8, 1751â1764 (2009).
van den Heuvel, S. & Harlow, E. Distinct roles for cyclin-dependent kinases in cell cycle control. Science 262, 2050â2054 (1993).
Nakatani, Y. & Ogryzko, V. Immunoaffinity purification of mammalian protein complexes. Methods Enzymol. 370, 430â444 (2003).
Tyanova, S., Temu, T. & Cox, J. The MaxQuant computational platform for mass spectrometry-based shotgun proteomics. Nat. Protoc. 11, 2301â2319 (2016).
Tyanova, S. et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat. Methods 13, 731â740 (2016).
Ritchie, M. E. et al. limma powers differential expression analyses for RNA-sequencing and microarray studies. Nucleic Acids Res. 43, e47 (2015).
R Core Team. R: a language and environment for statistical computing (2021).
Wickham, H. ggplot2: elegant graphics for data analysis (2016).
Slowikowski, K. ggrepel: automatically position non-overlapping text labels with âggplot2â (2018).
Wu, T. et al. clusterProfiler 4.0: a universal enrichment tool for interpreting omics data. Innovation 2, 100141 (2021).
Deutsch, E. W. et al. The ProteomeXchange consortium in 2020: enabling âbig dataâ approaches in proteomics. Nucleic Acids Res. 48, D1145âD1152 (2020).
Perez-Riverol, Y. et al. The PRIDE database and related tools and resources in 2019: improving support for quantification data. Nucleic Acids Res. 47, D442âD450 (2019).
Robinson, M. D., McCarthy, D. J. & Smyth, G. K. edgeR: a Bioconductor package for differential expression analysis of digital gene expression data. Bioinformatics 26, 139â140 (2010).
Nagahara, H. et al. Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration. Nat. Med. 4, 1449â1452 (1998).
Mirdita, M. et al. ColabFold: making protein folding accessible to all. Nat. Methods 19, 679â682 (2022).
Lu, C. et al. OPLS4: improving force field accuracy on challenging regimes of chemical space. J. Chem. Theory Comput. 17, 4291â4300 (2021).
Obenauer, J. C., Cantley, L. C. & Yaffe, M. B. Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31, 3635â3641 (2003).