PhD Scientific Days 2022

Molecular Sciences I. (Poster discussion will take place in the Aula during the Coffee Break)

Different Phosphorylation States of Native Full-length Titin Filaments Visualized by Atomic Force Microscopy

Előadó neve

Balogh-Molnár, Andrea

Előadó munkahelye

Department of Biophysics and Radiation Biology

Előadó telefonszáma

+36305608677

Előadó e-mail címe

balogh-molnar.andrea@med.semmelweis-univ.hu

Az előadás címe

Different Phosphorylation States of Native Full-length Titin Filaments Visualized by Atomic Force Microscopy

Szerző(k) neve és munkahelye

Andrea Balogh-Molnár1, Dominik Sziklai1, Zsolt Mártonfalvi1
1 Semmelweis University, Department of Biophysics and Radiation Biology

Bemutatás módja

Poszter

Szekció

Molecular Sciences I. (Poster discussion will take place in the Aula during the Coffee Break)

Language of the presentation

Hungarian

Preferred session

Molecular Sciences

Összefoglaló szövege

During muscle stretch, elastic or "passive" force develops which is mainly determined by the giant protein titin that forms the third filament system of muscle sarcomeres. The magnitude of this force is mainly dependent on the elasticity of the titin filaments, which is primarily determined by the structure of the polypeptide chain. However, it is suggested that post-translational modifications of titin, such as phosphokinase activity, regulate the sarcomeric passive force development. Mechanical studies on single myofibrils revealed that different protein kinases alter the passive tension of muscle, surprisingly, in opposite ways. This suggests that phosphorylation of sarcomeric proteins by various kinases is an essential regulatory mechanism of passive force. However, the extrapolation of these findings to titin’s phosphorylation has not been studied so far at the single-molecule level. To reveal titin’s contribution to the alterations of passive force due to phosphorylation, single-molecule experiments must be carried out on individual titin molecules, where the effect of each relevant phosphorylation state can be tested individually. In our work, we isolated individual full-length titin molecules from rabbit skeletal and cardiac muscle. The isolated native titin molecules showed high levels of phosphorylation, when stained with phosphoprotein gel stain. The isolated molecules were treated with various phosphatases and kinases to alter the in situ phosphorylation state of the polymer. To investigate the effect of the various phosphorylation states on titin's structure, we visualized surface-bound titin molecules by atomic force microscope and measured contour length to end-to-end length ratios of titin polymers.
This work is founded by the NKFIH FK128956 grant.

University and Doctoral School

Semmelweis University, Doctoral School of Theoretical and Translational Medicine

Supervisor

Zsolt Mártonfalvi

Publication of my abstract

I give consent to the publication of my abstract on the website of the congress.

Kind

Szabad

Status

elfogadva

Accepted presentation method

poszter

Előadás fájl jóváhagyás

nem rendelkezett róla

Előadó

6915

Start

11:30

End

11:35

Authors (legacy)

Andrea Balogh-Molnár1, Dominik Sziklai1, Zsolt Mártonfalvi1
1 Semmelweis University, Department of Biophysics and Radiation Biology