Author

S. N. Cullati

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Cell Biology· 2

Signature Assays, Organisms & Methods

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Research Focus:chromatin & epigenetic regulation· 4 Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Assay:proteomics· 2 Organism:yeast· 2 Research Focus:development & morphogenesis· 1 Organism:fungi (other)· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

J.-S. Chen· 4 shared K. L. Gould· 3 shared Z. C. Elmore· 2 shared A. E. Johnson· 1 shared C. M. Jones· 1 shared E. Zhang· 1 shared J. Navarrete-Perea· 1 shared J. R. Beckley· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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4 shared papersBiochemistry

J.-S. Chen

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4 papers

Recent·Most cited

Substrate displacement of CK1 C-termini regulates kinase specificity

S. N. Cullati, K. Akizuki, J.-S. Chen, K. N. Gould

The paper shows that autophosphorylated C-termini of CK1 kinases act as inhibitory pseudosubstrates, and their displacement by substrates regulates kinase specificity.

bioRxiv · Jun 30, 2023Biochemistry

Fission yeast CK1 promotes DNA double-strand break repair through both homologous recombination and non-homologous end joining

S. N. Cullati, E. Zhang, Y. Shan, R. X. Guillen, J.-S. Chen, J. Navarrete-Perea, Z. C. Elmore, L. Ren, S. P. Gygi, K. L. Gould

This study shows that fission yeast CK1 orthologues Hhp1 and Hhp2 promote DNA double-strand break repair through both homologous recombination and non-homologous end joining by phosphorylating substrates like Arp8.

bioRxiv · Apr 27, 2023 · PreprintCell Biology

Autophosphorylation of the CK1 kinase domain regulates enzyme activity and function

S. N. Cullati, J.-S. Chen, K. L. Gould

This study identifies a conserved autophosphorylation mechanism in CK1 kinases that inhibits activity, with implications for disease and regulation.

bioRxiv · Jun 5, 2019Biochemistry

Relief of the Dma1-mediated checkpoint requires Dma1 autoubiquitination and dynamic localization

C. M. Jones, J.-S. Chen, A. E. Johnson, Z. C. Elmore, S. N. Cullati, J. R. Beckley, K. L. Gould

This study shows that Dma1's transient removal from SPBs during anaphase B, driven by auto-ubiquitination, is essential for silencing the Dma1-dependent mitotic checkpoint in fission yeast.

bioRxiv · May 15, 2018Cell Biology