prikaz prve stranice dokumenta Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom
Embargo period 2025-02-28
master's thesis
Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom
Zagreb: University of Zagreb, Faculty of Science, 2023. urn:nbn:hr:217:656028
Ivanišević, Klara
University of Zagreb
Faculty of Science
Department of Biology

Institutional repository: Repository of the Faculty of Science

Cite this document

Ivanišević, K. (2023). Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:656028

Ivanišević, Klara. "Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom." Master's thesis, University of Zagreb, Faculty of Science, 2023. https://urn.nsk.hr/urn:nbn:hr:217:656028

Ivanišević, Klara. "Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom." Master's thesis, University of Zagreb, Faculty of Science, 2023. https://urn.nsk.hr/urn:nbn:hr:217:656028

Ivanišević, K. (2023). 'Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom', Master's thesis, University of Zagreb, Faculty of Science, accessed 23 December 2024, https://urn.nsk.hr/urn:nbn:hr:217:656028

Ivanišević K. Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2023 [cited 2024 December 23] Available at: https://urn.nsk.hr/urn:nbn:hr:217:656028

K. Ivanišević, "Uloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2023. Available at: https://urn.nsk.hr/urn:nbn:hr:217:656028

Metadata
TitleUloga fosfataze PGAM5 u mitofagiji posredovanoj BNIP3L/NIX receptorom
Title (english)Role of PGAM5 phosphatase in BNIP3L/NIX receptor-mediated mitophagia
AuthorKlara Ivanišević
MentorIvana Novak Nakir (mentor)
MentorNada Oršolić (komentor)
Committee memberNada Oršolić (predsjednik povjerenstva)
Committee memberSilvija Černi (član povjerenstva)
Committee memberJasna Lajtner (član povjerenstva)
Committee memberMaja Matulić (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Biology)
Zagreb
Defense date and country2023-02-28, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Biology
Abstract
Dosadašnja istraživanja su pokazala kako je dimerizacija receptora BNIP3L/NIX molekularni mehanizam koji pospješuje mitofagiju posredovanu receptorom. Stvaranjem homodimera, BNIP3L/NIX receptor pojačano regrutira autofagosome. Kako bi se razjasnio mehanizam dimerizacije, identificiran je serin na poziciji 212, kao najvažnija aminokiselina na Cterminalnom kraju BNIP3L/NIX receptora odgovorna za dimerizaciju. Eksperimentalno je pokazano da fosforilacija serina 212 sprječava stvaranje dimera BNIP3L/NIX receptora. Pretraživanjem literature definirane su potencijalne fosfataze C-terminalnog kraja receptora BNIP3L/NIX, a među njima je bila i fosfataza PGAM5 čije se djelovanje nastojalo istražiti. Cilj ovog istraživanja je bio otkriti ima li PGAM5 ulogu u defosforilaciji serina 212 što bi razjasnilo jedan od mehanizama regulacije mitofagije. Metodama pull-down i koimunoprecipitacije analizirana je interakcija fosfataze PGAM5 s fuzioniranim proteinom EGFP-BNIP3L/NIX i njegovim mutantama BNIP3L/NIX-S212A i BNIP3L/NIX-S212E. Dobiveni rezultati dokazali su interakciju receptora BNIP3L/NIX s fosfatazom PGAM5.
Abstract (english)
Previous research has shown that dimerization of the BNIP3L/NIX recepotr is a molecular mechanism that promotes receptor-mediated. Formation of a BNIP3L/NIX homodimer increases recruitment of mitochondria to autophagosomes. To elucidate the mechanism of dimerization, serine at position 212 was identified as the most important amino acid at the Cterminal end of the BNIP3L/NIX for dimerization. It was shown that serine 212 phosphorylation prevents the formation of BNIP3L/NIX dimers. By searching the literature, potential phosphatases of the C-terminal end of the BNIP3L/NIX receptor were defined, and among them was the PGAM5 phosphatase, whose activity was investigated in this master thesis. The aim of this research was to find whether PGAM5 has a role in the dephosphorylation of serine 212, which would clarify one of the mechanisms of mitophagy regulation. The interaction of the phosphatase PGAM5 with the fusion protein EGFP-BNIP3L/NIX and its mutants BNIP3L/NIX-S212A and BNIP3L/NIX-S212E was analyzed using pull-down and coimmunoprecipitation. The results have shown that BNIP3L/NIX is interacting with phosphatase PGAM5.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:656028
Study programmeTitle: Experimental Biology
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra eksperimentalne biologije (magistar/magistra eksperimentalne biologije)
Type of resourceText
File originBorn digital
Access conditionsEmbargoed access
Embargo expiration date: 2025-02-28
Terms of useLicence In copyright icon
Created on2023-03-08 11:41:00