PhD Scientific Days 2022

Budapest, 6-7 July 2022

Molecular Sciences III. (Poster discussion will take place on the terrace of the room during the Coffee Break)

Translocating proteins compartment-specifically alter the fate of epithelial-mesenchymal transition in a compartmentalized Boolean network model

Előadó neve

Dr. Mendik, Péter

Előadó munkahelye

Department of Molecular Biology

Előadó telefonszáma

+36304740319

Előadó e-mail címe

petermendik@gmail.com

Az előadás címe

Translocating proteins compartment-specifically alter the fate of epithelial-mesenchymal transition in a compartmentalized Boolean network model

Szerző(k) neve és munkahelye

Péter Mendik1#, Márk Kerestély1#, Sebestyén Kamp2, Dávid Deritei1, Nina Kunšič1, Zsolt Vassy1, Péter Csermely1, Daniel V. Veres1,2

1Department of Molecular Biology, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary
2Turbine Ltd. Budapest, Hungary

#The authors wish it to be known, that the first two authors should be regarded as Joint First Authors.

Bemutatás módja

Szóbeli

Szekció

Molecular Sciences III. (Poster discussion will take place on the terrace of the room during the Coffee Break)

Language of the presentation

English

Preferred session

Molecular Sciences

Összefoglaló szövege

Epithelial-mesenchymal transition (EMT) plays a pivotal role in cellular processes, such as embryonic development, wound healing or cancer progression. Amongst orchestrators of EMT we can find several translocating proteins, such as key transcription factors (e.g.: β-catenin). The regulation of translocating proteins defines cellular behaviour.
We described how protein translocation generally affects cellular regulation through systematically incorporating protein translocation into an in silico Boolean dynamic signalling model.
Highlighting their role, translocating proteins become enriched in EMT-signalling. We created a compartmentalized Boolean network model in order to simulate the compartment-specific functions of translocating proteins.
Our model reproduced known biological traits of EMT and as a novel feature it also captured organelle-specific functions of proteins. Our results predicted that glycogen synthase kinase-3 beta (GSK3B) compartment-specifically alters the fate of EMT and among others the activation of nuclear GSK3B halts transforming growth factor beta-1 (TGFB) induced EMT. Moreover, our results recapitulated that the nuclear activation of glioma associated oncogene transcription factors (GLI) is needed to achieve a complete EMT. Compartmentalized network models similar to ours, will be useful to understand subcellular processes and to create more complex drug targeting strategies.
This work was supported by the ÚNKP-20-III-2-SE-23 New National Excellence Program of the Ministry for Innovation and Technology from the source of the National Research, Development and Innovation fund, through the EFOP-3.6.3-VEKOP-16-2017-00009 (titled: “Az orvos-, egészségtudományi- és gyógyszerészképzés tudományos műhelyeinek fejlesztése) programme, by the Hungarian National Research, Development and Innovation Office [K131458], by the Higher Education Institutional Excellence Programme of the Ministry of Human Capacities in Hungary, within the framework of the Molecular Biology thematic programmes of Semmelweis University, by the Thematic Excellence Programme (Tématerületi Kiválósági Program, 2020-4.1.1.-TKP2020, TKP-2021-EGA-24) of the Ministry for Innovation and Technology in Hungary, within the framework of the Molecular Biology thematic programme of the Semmelweis University.

University and Doctoral School

Semmelweis University, Doctoral School of Molecular Medicine

Supervisor

Prof Péter Csermely, Dániel Veres MD PhD

Publication of my abstract

I do not give consent to the publication of my abstract on the website of the congress.

Kind

Szabad

Status

elfogadva

Accepted presentation method

szóbeli

Előadás fájl jóváhagyás

nem rendelkezett róla

Előadó

4782

Start

12:15

End

12:30

Authors (legacy)

Péter Mendik1#, Márk Kerestély1#, Sebestyén Kamp2, Dávid Deritei1, Nina Kunšič1, Zsolt Vassy1, Péter Csermely1, Daniel V. Veres1,2

1Department of Molecular Biology, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary
2Turbine Ltd. Budapest, Hungary

#The authors wish it to be known, that the first two authors should be regarded as Joint First Authors.