Összes szerző


Månsson, Alf

az alábbi absztraktok szerzői között szerepel:

Huber Tamás
Comparative Analyses of the Gelsolin Homology Domains of Gelsolin and Flightless-I

Aug 29 - kedd

15:30 – 17:00

I. Poszterszekció

P14

Comparative Analyses of the Gelsolin Homology Domains of Gelsolin and Flightless-I

Tamás Huber1,3, Péter Gaszler1,3, Veronika Takács-Kollár1, Réka Pintér1, Rauan Sakenov1, Andrea Teréz Vig1, Mónika Ágnes Tóth1, Venukumar Vemula2, Marko Ušaj2, Alf Månsson2 and Beáta Bugyi1,3

1University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, Pécs, H-7624, Hungary

2Linnaeus University, Department of Chemistry and Biomedical Sciences, SE-39182, Kalmar, Sweden

3Regional Committee of The Hungarian Academy of Sciences at Pécs, The Expert Committee of Physics and Astronomy, Spectroscopy Committee

Flightless-I is a unique member of the gelsolin (GSN) superfamily alloying six gelsolin homology (GH) domains and leucine-rich repeats. Flightless-I is an established regulator of the actin cytoskeleton. However, its biochemical activities in actin dynamics regulation are still largely elusive. To better understand its biological functioning, we performed a comparative analysis of GSN and Flightless-I by in vitro fluorescence spectroscopy and single filament TIRF microscopy approaches. We found that Flightless-I can interact with actin and affect actin dynamics in a calcium-independent fashion. Notably, our functional analyses indicate that GSN and Flightless-I respond to calcium differently implying different conformational characteristics of the GH domains in the two proteins. Bioinformatics analyses predict that the sequence elements responsible for calcium activation of GSN are not conserved in the GH domains of Flightless-I. Consistently, the use of intrinsic and extrinsic fluorescent probes revealed that unlike that of GSN the conformational behavior of the GH domains Flightless-I was not significantly affected by calcium-binding. Altogether, our work reveals different calcium-response and predicts distinct modes of activation of GSN and Flightless-I.

Acknowledgment

Activities of Flightless I revealed by acto-myosin based in vitro motility techniques, 2021-4.1.2-NEMZ_KI-2022-00025 (TH); New National Excellence Program of the Ministry for Innovation and Technology ÚNKP-21-3-II-PTE-997 (PG). We thank József Mihály (Institute of Genetics, Biological Research Centre) for the Drosophila Flightless-I plasmids, Tomohito Higashi (Fukushima Medical University) for the human Flightless-I plasmids and Robert C. Robinson (Okoyama University) for the human GSN plasmid.