Thesis supervisor: Mónika Gönczi
Location of studies (in Hungarian): Department of Physiology, Faculty of Medicine, University of Debrecen Abbreviation of location of studies: DEÉI
Description of the research topic:
Septins are small GTP-binding proteins of 30-65 kDa that is highly conserved in eukaryotes and control cellular processes by polymerizing into hetero-oligomeric protein complexes that can further form filaments. Septins have been recognized as a cytoskeletal components because of their filamentous appearance, as well as their association with cellular membranes, actin filaments and microtubules. The expanding number of functional studies has shown that septins orchestrate a range of key cellular processes, including cytokinesis, ciliogenesis and neurogenesis, by serving as scaffolds for protein recruitment and/or as a diffusion barriers to compartmentalize discrete cellular domains. An increasing number of data implicates the role of septin family in the pathogenesis of diverse diseases. According expeimental results septins has crutial role in organizing a highly localized plasma membrane domains that are important in STIM1-ORAI1 signaling and in the mechanism of store-operated calcium entry (SOCE), and also indicate that septins may organize membrane microdomains relevant to other signaling processes. The exact functional role of septins in skeletal muscle has not well characterized, so our research want to point out their role in the calcium homeostasis and development of skeletal muscle. It has already known that septin 7 isoform is present in all hexamer or octamer formation, so we are keen on to provide useful information about the role of septin 7 both in cultured skeletal muscle cell line and in vivo isolated muscle fibers.
Required language skills: angol középfok Number of students who can be accepted: 1
Deadline for application: 2018-05-15
2024. IV. 17. ODT ülés Az ODT következő ülésére 2024. június 14-én, pénteken 10.00 órakor kerül sor a Semmelweis Egyetem Szenátusi termében (Bp. Üllői út 26. I. emelet).
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