We investigate how cells robustly execute cell division, a process that is highly dynamic and requires intricate regulation. The group combines quantitative perturbations, live cell imaging, and computational modeling to understand the underlying regulation.



Principal Investigators

Silke Hauf

Fellow and Assistant Professor



Carpy A, Koch A, Bicho CC, et al. Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)-Based Quantitative Proteomics and Phosphoproteomics in Fission Yeast. Cold Spring Harb Protoc. 2017;2017(6):pdb prot091686.  https://www.ncbi.nlm.nih.gov/pubmed/28572185

Ciliberto A, Hauf S. Micromanaging checkpoint proteins. Elife. 2017;6.  https://www.ncbi.nlm.nih.gov/pubmed/28206949

Kamenz J, Hauf S. Time To Split Up: Dynamics of Chromosome Separation. Trends Cell Biol. 2017;27(1):42–54.  https://www.ncbi.nlm.nih.gov/pubmed/27567180

Koch A, Bicho CC, Borek WE, et al. Construction, Growth, and Harvesting of Fission Yeast Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) Strains. Cold Spring Harb Protoc. 2017;2017(6):pdb prot091678.  https://www.ncbi.nlm.nih.gov/pubmed/28572184

Macek B, Carpy A, Koch A, et al. Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) Technology in Fission Yeast. Cold Spring Harb Protoc. 2017;2017(6):pdb top079814.  https://www.ncbi.nlm.nih.gov/pubmed/28572211

Sewart K, Hauf S. Different Functionality of Cdc20 Binding Sites within the Mitotic Checkpoint Complex. Curr Biol. 2017;27(8):1213–1220.  https://www.ncbi.nlm.nih.gov/pubmed/28366743


Geissen EM, Hasenauer J, Heinrich S, Hauf S, Theis FJ, Radde N. MEMO – Multi-experiment mixture model analysis of censored data. Bioinformatics. 2016.  http://www.ncbi.nlm.nih.gov/pubmed/27153627


Kamenz J, Mihaljev T, Kubis A, Legewie S, Hauf S. Robust Ordering of Anaphase Events by Adaptive Thresholds and Competing Degradation Pathways. Mol Cell. 2015;60(3):446–459.  http://www.ncbi.nlm.nih.gov/pubmed/26527280


Carpy A, Krug K, Graf S, et al. Absolute proteome and phosphoproteome dynamics during the cell cycle of fission yeast. Mol Cell Proteomics. 2014;13(8):1925–36.  http://www.ncbi.nlm.nih.gov/pubmed/24763107

Heinrich S, Sewart K, Windecker H, et al. Mad1 contribution to spindle assembly checkpoint signalling goes beyond presenting Mad2 at kinetochores. EMBO Rep. 2014;15:291–298.  http://www.ncbi.nlm.nih.gov/pubmed/24477934

Kamenz J, Hauf S. Slow checkpoint activation kinetics as a safety device in anaphase. Curr Biol. 2014;24:646–651.  http://www.ncbi.nlm.nih.gov/pubmed/24583014


Hauf S. The spindle assembly checkpoint: progress and persistent puzzles. Biochem Soc Trans. 2013;41:1755–1760.  http://www.ncbi.nlm.nih.gov/pubmed/24256287

Heinrich S, Geissen EM, Kamenz J, et al. Determinants of robustness in spindle assembly checkpoint signalling. Nat Cell Biol. 2013;15:1328–1339.  http://www.ncbi.nlm.nih.gov/pubmed/24161933


Heinrich S, Windecker H, Hustedt N, Hauf S. Mph1 kinetochore localization is crucial and upstream in the hierarchy of spindle assembly checkpoint protein recruitment to kinetochores. J Cell Sci. 2012;125:4720–4727.  http://www.ncbi.nlm.nih.gov/pubmed/22825872

Koch A, Rode HB, Richters A, Rauh D, Hauf S. A chemical genetic approach for covalent inhibition of analogue-sensitive aurora kinase. ACS Chem Biol. 2012;7:723–731.  http://www.ncbi.nlm.nih.gov/pubmed/22264160


Koch A, Krug K, Pengelley S, Macek B, Hauf S. Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast. Sci Signal. 2011;4:rs6.  http://www.ncbi.nlm.nih.gov/pubmed/21712547

Sakuno T, Tanaka K, Hauf S, Watanabe Y. Repositioning of aurora B promoted by chiasmata ensures sister chromatid mono-orientation in meiosis I. Dev Cell. 2011;21:534–545.  http://www.ncbi.nlm.nih.gov/pubmed/21920317


Koch A, Hauf S. Strategies for the identification of kinase substrates using analog-sensitive kinases. Eur J Cell Biol. 2010;89:184–193.  http://www.ncbi.nlm.nih.gov/pubmed/20061049


Windecker H, Langegger M, Heinrich S, Hauf S. Bub1 and Bub3 promote the conversion from monopolar to bipolar chromosome attachment independently of shugoshin. EMBO Rep. 2009;10:1022–1028.  http://www.ncbi.nlm.nih.gov/pubmed/19680287


Hauf S. Mps1 checks up on chromosome attachment. Cell. 2008;132:181–182.  http://www.ncbi.nlm.nih.gov/pubmed/18243093


Hauf S, Biswas A, Langegger M, Kawashima SA, Tsukahara T, Watanabe Y. Aurora controls sister kinetochore mono-orientation and homolog bi-orientation in meiosis-I. Embo J. 2007;26:4475–4486.  http://www.ncbi.nlm.nih.gov/pubmed/17932486

Kawashima SA, Tsukahara T, Langegger M, Hauf S, Kitajima TS, Watanabe Y. Shugoshin enables tension-generating attachment of kinetochores by loading Aurora to centromeres. Genes Dev. 2007;21:420–435.  http://www.ncbi.nlm.nih.gov/pubmed/17322402


Hauf S, Roitinger E, Koch B, Dittrich CM, Mechtler K, Peters JM. Dissociation of cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2. PLoS Biol. 2005;3:e69.  http://www.ncbi.nlm.nih.gov/pubmed/15737063

Kitajima TS, Hauf S, Ohsugi M, Yamamoto T, Watanabe Y. Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization. Curr Biol. 2005;15:353–359.  http://www.ncbi.nlm.nih.gov/pubmed/15723797


Gimenez-Abian JF, Sumara I, Hirota T, et al. Regulation of sister chromatid cohesion between chromosome arms. Curr Biol. 2004;14:1187–1193.  http://www.ncbi.nlm.nih.gov/pubmed/15242616

Hauf S, Watanabe Y. Kinetochore orientation in mitosis and meiosis. Cell. 2004;119:317–327.  http://www.ncbi.nlm.nih.gov/pubmed/15507205


Hauf S. Fine tuning of kinetochore function by phosphorylation. Cell Cycle. 2003;2:228–229.  http://www.ncbi.nlm.nih.gov/pubmed/12734430

Hauf S, Cole RW, LaTerra S, et al. The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint. J Cell Biol. 2003;161:281–294.  http://www.ncbi.nlm.nih.gov/pubmed/12707311


Hauf S, Waizenegger IC, Peters JM. Cohesin cleavage by separase required for anaphase and cytokinesis in human cells. Science. 2001;293:1320–1323.  http://www.ncbi.nlm.nih.gov/pubmed/11509732


Waizenegger IC, Hauf S, Meinke A, Peters JM. Two distinct pathways remove mammalian cohesin from chromosome arms in prophase and from centromeres in anaphase. Cell. 2000;103:399–410.  http://www.ncbi.nlm.nih.gov/pubmed/11081627