Plasma Membrane Protein Nce102 Modulates Morphology and Function of the Yeast Vacuole

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378041%3A_____%2F20%3A00539319" target="_blank" >RIV/68378041:_____/20:00539319 - isvavai.cz</a>

Result on the web

<a href="https://www.mdpi.com/2218-273X/10/11/1476" target="_blank" >https://www.mdpi.com/2218-273X/10/11/1476</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/biom10111476" target="_blank" >10.3390/biom10111476</a>

Result language

angličtina

Original language name

Plasma Membrane Protein Nce102 Modulates Morphology and Function of the Yeast Vacuole

Original language description

Membrane proteins are targeted not only to specific membranes in the cell architecture, but also to distinct lateral microdomains within individual membranes to properly execute their biological functions. Yeast tetraspan protein Nce102 has been shown to migrate between such microdomains within the plasma membrane in response to an acute drop in sphingolipid levels. Combining microscopy and biochemistry methods, we show that upon gradual ageing of a yeast culture, when sphingolipid demand increases, Nce102 migrates from the plasma membrane to the vacuole. Instead of being targeted for degradation it localizes to V-ATPase-poor, i.e., ergosterol-enriched, domains of the vacuolar membrane, analogous to its plasma membrane localization. We discovered that, together with its homologue Fhn1, Nce102 modulates vacuolar morphology, dynamics, and physiology. Specifically, the fusing of vacuoles, accompanying a switch of fermenting yeast culture to respiration, is retarded in the strain missing both proteins. Furthermore, the absence of either causes an enlargement of ergosterol-rich vacuolar membrane domains, while the vacuoles themselves become smaller. Our results clearly show decreased stability of the V-ATPase in the absence of either Nce102 or Fhn1, a possible result of the disruption of normal microdomain morphology of the vacuolar membrane. Therefore, the functionality of the vacuole as a whole might be compromised in these cells.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10601 - Cell biology

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

Publication year

2020

Confidentiality

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

Name of the periodical

Biomolecules

ISSN

2218-273X

e-ISSN

—

Volume of the periodical

10

Issue of the periodical within the volume

11

Country of publishing house

CH - SWITZERLAND

Number of pages

18

Pages from-to

1476

UT code for WoS article

000592898200001

EID of the result in the Scopus database

2-s2.0-85094821820