The lipid droplet protein Pgc1 controls the subcellular distribution of phosphatidylglycerol

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378041%3A_____%2F19%3A00517826" target="_blank" >RIV/68378041:_____/19:00517826 - isvavai.cz</a>

Výsledek na webu

<a href="https://academic.oup.com/femsyr/article-abstract/19/5/foz045/5524364?redirectedFrom=fulltext" target="_blank" >https://academic.oup.com/femsyr/article-abstract/19/5/foz045/5524364?redirectedFrom=fulltext</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/femsyr/foz045" target="_blank" >10.1093/femsyr/foz045</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The lipid droplet protein Pgc1 controls the subcellular distribution of phosphatidylglycerol

Popis výsledku v původním jazyce

The biosynthesis of yeast phosphatidylglycerol (PG) takes place in the inner mitochondrial membrane. Outside mitochondria, the abundance of PG is low. Here, we present evidence that the subcellular distribution of PG is maintained by the locally controlled enzymatic activity of the PG-specific phospholipase, Pgc1. A fluorescently labeled Pgc1 protein accumulates on the surface of lipid droplets (LD). We show, however, that LD are not only dispensable for Pgc1-mediated PG degradation, but do not even host any phospholipase activity of Pgc1. Our in vitro assays document the capability of LD-accumulated Pgc1 to degrade PG upon entry to the membranes of the endoplasmic reticulum, mitochondria and even of artificial phospholipid vesicles. Fluorescence recovery after photobleaching analysis confirms the continuous exchange of GFP-Pgc1 within the individual LD in situ, suggesting that a steady-state equilibrium exists between LD and membranes to regulate the immediate phospholipase activity of Pgc1. In this model, LD serve as a storage place and shelter Pgc1, preventing its untimely degradation, while both phospholipase activity and degradation of the enzyme occur in the membranes. nnThe levels of a cardiolipin precursor PG are kept low outside mitochondria in yeast cells by the spatially confined activity of the PG specific phospholipase C, Pgc1.

Název v anglickém jazyce

The lipid droplet protein Pgc1 controls the subcellular distribution of phosphatidylglycerol

Popis výsledku anglicky

The biosynthesis of yeast phosphatidylglycerol (PG) takes place in the inner mitochondrial membrane. Outside mitochondria, the abundance of PG is low. Here, we present evidence that the subcellular distribution of PG is maintained by the locally controlled enzymatic activity of the PG-specific phospholipase, Pgc1. A fluorescently labeled Pgc1 protein accumulates on the surface of lipid droplets (LD). We show, however, that LD are not only dispensable for Pgc1-mediated PG degradation, but do not even host any phospholipase activity of Pgc1. Our in vitro assays document the capability of LD-accumulated Pgc1 to degrade PG upon entry to the membranes of the endoplasmic reticulum, mitochondria and even of artificial phospholipid vesicles. Fluorescence recovery after photobleaching analysis confirms the continuous exchange of GFP-Pgc1 within the individual LD in situ, suggesting that a steady-state equilibrium exists between LD and membranes to regulate the immediate phospholipase activity of Pgc1. In this model, LD serve as a storage place and shelter Pgc1, preventing its untimely degradation, while both phospholipase activity and degradation of the enzyme occur in the membranes. nnThe levels of a cardiolipin precursor PG are kept low outside mitochondria in yeast cells by the spatially confined activity of the PG specific phospholipase C, Pgc1.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

<a href="/cs/project/GA19-04052S" target="_blank" >GA19-04052S: Funkce specifických membránových mikrodomén v homeostáze lipidů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

FEMS Yeast Research

ISSN

1567-1356

e-ISSN

—

Svazek periodika

19

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

foz045

Kód UT WoS článku

000483813700004

EID výsledku v databázi Scopus

2-s2.0-85069625327