Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00484574" target="_blank" >RIV/61388971:_____/17:00484574 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1038/cddiscovery.2017.16" target="_blank" >http://dx.doi.org/10.1038/cddiscovery.2017.16</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/cddiscovery.2017.16" target="_blank" >10.1038/cddiscovery.2017.16</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets

Popis výsledku v původním jazyce

In recent years it turned out that there is not only extensive communication between the nucleus and mitochondria but also between mitochondria and lipid droplets (LDs) as well. We were able to demonstrate that a number of proteins shuttle between LDs and mitochondria and it depends on the metabolic state of the cell on which organelle these proteins are predominantly localized. Responsible for the localization of the particular proteins is a protein domain consisting of two alfa-helices, which we termed V-domain according to the predicted structure. So far we have detected this domain in the following proteins: mammalian BAX, BCL-XL, TCTP and yeast Mmi1p and Erg6p. According to our experiments there are two functions of this domain: (1) shuttling of proteins to mitochondria in times of stress and apoptosis, (2) clearing the outer mitochondrial membrane from pro- as well as anti-apoptotic proteins by moving them to LDs after the stress ceases. In this way the LDs are used by the cell to modulate stress response.

Název v anglickém jazyce

Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets

Popis výsledku anglicky

In recent years it turned out that there is not only extensive communication between the nucleus and mitochondria but also between mitochondria and lipid droplets (LDs) as well. We were able to demonstrate that a number of proteins shuttle between LDs and mitochondria and it depends on the metabolic state of the cell on which organelle these proteins are predominantly localized. Responsible for the localization of the particular proteins is a protein domain consisting of two alfa-helices, which we termed V-domain according to the predicted structure. So far we have detected this domain in the following proteins: mammalian BAX, BCL-XL, TCTP and yeast Mmi1p and Erg6p. According to our experiments there are two functions of this domain: (1) shuttling of proteins to mitochondria in times of stress and apoptosis, (2) clearing the outer mitochondrial membrane from pro- as well as anti-apoptotic proteins by moving them to LDs after the stress ceases. In this way the LDs are used by the cell to modulate stress response.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Cell Death Discovery

ISSN

2058-7716

e-ISSN

—

Svazek periodika

3

Číslo periodika v rámci svazku

March 20

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

12

Strana od-do

17016

Kód UT WoS článku

000463082900029

EID výsledku v databázi Scopus

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