The lipid droplet protein Pgc1 controls the subcellular distribution of phosphatidylglycerol
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
The lipid droplet protein Pgc1 controls the subcellular distribution of phosphatidylglycerol
Original language description
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.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10601 - Cell biology
Result continuities
Project
<a href="/en/project/GA19-04052S" target="_blank" >GA19-04052S: Function of specific membrane microdomains in lipid homeostasis</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEMS Yeast Research
ISSN
1567-1356
e-ISSN
—
Volume of the periodical
19
Issue of the periodical within the volume
5
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
foz045
UT code for WoS article
000483813700004
EID of the result in the Scopus database
2-s2.0-85069625327