The cheerio mechanosensory region fine-tunes Drosophila cellularization

Drosophila melanogasterin alkiovaiheen aikana tapahtuvassa soluuntumisessa on mukana useita eri aktiinisäikeitä yhteenliittäviä proteiineja, jotka kontrolloivat aktomyosiinirenkaan muotoa ja kokoa. Filamiinin ortologi cheerio on yksi näistä proteiineista. Sen karboksipäässä on mekanosensorinen alue,...

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Main Author: Hakanen, Mikko
Other Authors: Matemaattis-luonnontieteellinen tiedekunta, Faculty of Sciences, Bio- ja ympäristötieteiden laitos, Department of Biological and Environmental Science, Jyväskylän yliopisto, University of Jyväskylä
Format: Master's thesis
Language:eng
Published: 2024
Subjects:
Online Access: https://jyx.jyu.fi/handle/123456789/96102
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author Hakanen, Mikko
author2 Matemaattis-luonnontieteellinen tiedekunta Faculty of Sciences Bio- ja ympäristötieteiden laitos Department of Biological and Environmental Science Jyväskylän yliopisto University of Jyväskylä
author_facet Hakanen, Mikko Matemaattis-luonnontieteellinen tiedekunta Faculty of Sciences Bio- ja ympäristötieteiden laitos Department of Biological and Environmental Science Jyväskylän yliopisto University of Jyväskylä Hakanen, Mikko Matemaattis-luonnontieteellinen tiedekunta Faculty of Sciences Bio- ja ympäristötieteiden laitos Department of Biological and Environmental Science Jyväskylän yliopisto University of Jyväskylä
author_sort Hakanen, Mikko
datasource_str_mv jyx
description Drosophila melanogasterin alkiovaiheen aikana tapahtuvassa soluuntumisessa on mukana useita eri aktiinisäikeitä yhteenliittäviä proteiineja, jotka kontrolloivat aktomyosiinirenkaan muotoa ja kokoa. Filamiinin ortologi cheerio on yksi näistä proteiineista. Sen karboksipäässä on mekanosensorinen alue, joka sisältää kaksi peitettyä proteiinin vuorovaikutuspaikkaa. Tämän alueen rooli soluuntumisessa ei ole vielä täysin selvillä. Kokeessa käytettiin kolmea eri kärpäslinjaa, jotka vaihtelivat proteiinien vuorovaikutuspaikkojen saavutettavuuden helppoudessa. Alkion soluuntumista kuvattiin elävistä alkioista. Konfokaali mikroskoopi pinoja otettiin 3 minuutin välein ja cheerion sijoittumista sekä aktomyosiinirengasta soluuntumisen aikana seurattiin GFP-tunnisteen avulla. Linja, jonka proteiinin vuorovaikutusalue oli vähiten peitetty, erottui muista linjoista renkaan kehän pituuden ja pyöreyden, sekä cheerion sijoittumisen suhteen. Tämän linjan renkaiden kehän pituus pysyi muita linjoja suurempana koko soluuntumisen ajan, kun taas linjan renkaiden pyöreys laski myöhäisen soluuntumisen aikana. Iso osa cheerio proteiineista tämän linjan soluuntumisessa sijoittuivat pois aktiinimyosiinirenkaiden luota. Tulosten perusteella vaikuttaa siltä, että cheerion mekanosensoriselle alueelle on jonkinlainen vaikutus aktomyosiinirenkaaseen, joko suoraan tai epäsuorasti. Suoraan vaikuttamalla renkaiden muotoon ja supistumiseen tai epäsuorasti muiden vuorovaikutusten kanssa. Tulokset sopivat yhteen aikaisempiin tutkimustuloksiin, joiden mukaan mekanosensorinen alue on vastuussa filamiinin interaktiosta solukalvon proteiinien kanssa ja näin myös tämän kiinnittymisestä solukalvoon. Tätä kautta cheerion mekanosensorinen alue näyttää myös kontrolloivan cheerion lokalisaatiota. Cellularization, a process in the Drosophila melanogaster's embryo stage requires actomyosin polymerization and contraction for membrane invagination and formation of individual cells after multiple mitosis. To accomplish this cellularization utilizes different actin crosslinkers to control the shape and size of actomyosin rings. One of these actin crosslinkers is cheerio, an orthologue of filamin, which contains a mechanosensory region with two masked protein interaction sites in its C-terminal. The role of this region in cellularization is not yet clear. Cellularization from three different fly lineages, which differed in the ease of access to their protein interaction sites, was imaged from living embryos. Confocal microscopy stacks were taken with 3-minute intervals and the localization of cheerio at the actomyosin ring was followed with a GFP tag. The genotype with the least restriction to its protein interaction site separated itself from other genotypes by its perimeter and circularity values and by being localized differently. It obtained larger perimeter length values throughout the cellularization process and decreased in circularity values through the late cellularization. This genotype also had most of its cheerio localized away from the actomyosin rings. These results suggest that the cheerio mechanosensory region affect the actomyosin rings during cellularization, either directly by altering their conformation and contraction, or indirectly by localizing cheerio away from the rings and letting the process complete without the crosslinker’s influence. The results are also in accordance with previous filamin studies suggesting that the mechanosensory region is responsible for the filamins attachment to membrane through transmembrane protein interaction. Based on this the mechanosensory region of cheerio seems to also control the localization of cheerio.
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spellingShingle Hakanen, Mikko The cheerio mechanosensory region fine-tunes Drosophila cellularization Actin crosslinker Actomyosin Filamin Solu- ja molekyylibiologia Cell and molecular biology 4013 proteiinit filamiinit solukalvot aktomyosiini aktiinit alkio proteins filamins cell membranes actomyosin actins embryo
title The cheerio mechanosensory region fine-tunes Drosophila cellularization
title_full The cheerio mechanosensory region fine-tunes Drosophila cellularization
title_fullStr The cheerio mechanosensory region fine-tunes Drosophila cellularization The cheerio mechanosensory region fine-tunes Drosophila cellularization
title_full_unstemmed The cheerio mechanosensory region fine-tunes Drosophila cellularization The cheerio mechanosensory region fine-tunes Drosophila cellularization
title_short The cheerio mechanosensory region fine-tunes Drosophila cellularization
title_sort cheerio mechanosensory region fine tunes drosophila cellularization
title_txtP The cheerio mechanosensory region fine-tunes Drosophila cellularization
topic Actin crosslinker Actomyosin Filamin Solu- ja molekyylibiologia Cell and molecular biology 4013 proteiinit filamiinit solukalvot aktomyosiini aktiinit alkio proteins filamins cell membranes actomyosin actins embryo
topic_facet 4013 Actin crosslinker Actomyosin Cell and molecular biology Filamin Solu- ja molekyylibiologia actins actomyosin aktiinit aktomyosiini alkio cell membranes embryo filamiinit filamins proteiinit proteins solukalvot
url https://jyx.jyu.fi/handle/123456789/96102 http://www.urn.fi/URN:NBN:fi:jyu-202406244949
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