Dr. Katarzyna Kliza

Dr. Katarzyna Kliza

Max-Planck-Forschungsgruppenleiterin

Decoding Post-Translational Modification Signalling Networks


Overview

Successful cellular adaptation to continuously changing environmental conditions relies on intricate regulatory mechanisms. Post-translational modifications (PTMs) represent a key strategy to ensure a dynamic, specific and accurate cellular response to external and internal stimuli. These chemical modifications regulate all aspects of a protein’s life, such as folding, trafficking, interactions, and (enzymatic) activity. Hitherto, hundreds of different PTMs have been discovered and their associations with diverse human maladies are well-documented. Nevertheless, due to their complexity and intricate crosstalk, our understanding of the features and molecular and (patho)physiological roles of PTMs is far from being complete. Our group focuses on elucidating the fundamental mechanisms and the physiological relevance of PTM signalling networks, focusing on ADP-ribosylation. Towards this aim, we employ a multifaceted and interdisciplinary approach, including proteomics, biochemistry, molecular and cell biology techniques.

 

Publications

ORCID List

2024

Kliza, K.W.*, #, Song, W.*, Pinzuti, I., Schaubeck, S., Kunzelmann, S., Kuntin, D., Fornili, A., Pandini, A., Hofmann, K., Garnett, J.A., Stieglitz, B.#, and Husnjak, K.#(2024) N4BP1 functions as a dimerization-dependent linear ubiquitin reader which regulates TNF signalling. Cell Death Discov.
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2023

Llerena Schiffmacher DA*, Lee SH*, Kliza KW, Theil AF, Akita M, Helfricht A, Bezstarosti K, Gonzalo-Hansen, C, van Attikum H, Verlaan-de Vries M, Vertegaal A, Hoeijmakers J, Marteijn J, Lans H, Demmers JAA, Vermeulen, M, Sixma, T, Ogi T, Vermeulen W#, and Pines A.#(2023). DDA1, a novel factor in transcription-coupled repair, modulates CRL4CSA dynamics at DNA damage-stalled RNA polymerase II. In revision. 

Llerena Schiffmacher DA, Kliza KW, Theil AF, Kremers GJ, Demmers JAA, Ogi T, Vermeulen M., Vermeulen W# and Pines A# (2023). Live cell transcription-coupled nucleotide excision repair dynamics revisitedDNA Repair (Amst)
Source

 

Neikes HK, Kliza KW, Gräwe C, Wester RA, Jansen PWTC, Lamers, LA, Baltissen MP, van Heeringen SJ, Logie C, Teichmann SA, Lindeboom RGH# and Vermeulen M# (2023) Quantification of absolute transcription-factor binding affinities in the native chromatin context using BANC-seq. Nat Biotechnol 
Source

Llerena Schiffmacher DA*, Lee SH*, Kliza KW, Theil AF, Akita M, Helfricht A, Bezstarosti K, Gonzalo-Hansen, C, van Attikum H, Verlaan-de Vries M, Vertegaal A, Hoeijmakers J, Marteijn J, Lans H, Demmers JAA, Vermeulen, M, Sixma, T, Ogi T, Vermeulen W#, and Pines A.#(2023). DDA1, a novel factor in transcription-coupled repair, modulates CRL4CSA dynamics at DNA damage-stalled RNA polymerase II. In revision. 

Llerena Schiffmacher DA, Kliza KW, Theil AF, Kremers GJ, Demmers JAA, Ogi T, Vermeulen M., Vermeulen W# and Pines A# (2023). Live cell transcription-coupled nucleotide excision repair dynamics revisitedDNA Repair (Amst) 
Source

2021

Kliza, K.*#, Liu, Q.*, Roosenboom, L.R.M., Filippov, D.V.# and Vermeulen, M.# (2021) Reading ADP-ribosylation signalling using chemical biology and interaction proteomics. Mol Cell
Source

Kliza, K.*#, Song, W.*, Pinzuti, I., Schaubeck, S., Kunzelmann, S., Kuntin, D., Fornili, A., Pandini, A., Hofmann, K., Garnett, J.A., Stieglitz, B.#, and Husnjak, K.# (2021) N4BP1 is dimerization-dependent linear ubiquitin reader regulating TNFR1 signalling through linear ubiquitin binding and Caspase-8-mediated processing. bioRxiv
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2020

Kliza, K.# and Husnjak, K.# (2020) Resolving the complexity of ubiquitin networks. Front Mol Biosci
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2017

Kliza, K., Taumer, C., Pinzuti, I., Franz-Wachtel, M., Kunzelmann, S., Stieglitz, B., Macek, B., and Husnjak, K. (2017) Internally tagged ubiquitin: a tool to identify linear polyubiquitin-modified proteins by mass spectrometry. Nat Methods
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2015

Leznicki, P.*, Korac-Prlic, J.*, Kliza, K., Husnjak, K., Nyathi, Y., Dikic, I., and High, S. (2015) Binding of SGTA to Rpn13 selectively modulates protein quality control. J Cell Sci
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* Co-first authors
# Co-corresponding authors

Equally contributed authors

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