PI(4,5)P-2 controls plasma membrane PI4P and PS levels via ORP5/8 recruitment to ER-PM contact sites

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00490854" target="_blank" >RIV/61388963:_____/18:00490854 - isvavai.cz</a>

Výsledek na webu

<a href="http://jcb.rupress.org/content/217/5/1797" target="_blank" >http://jcb.rupress.org/content/217/5/1797</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1083/jcb.201710095" target="_blank" >10.1083/jcb.201710095</a>

Jazyk výsledku

angličtina

Název v původním jazyce

PI(4,5)P-2 controls plasma membrane PI4P and PS levels via ORP5/8 recruitment to ER-PM contact sites

Popis výsledku v původním jazyce

Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P-2) is a critically important regulatory lipid of the plasma membrane (PM), however, little is known about how cells regulate PM PI(4,5)P-2 levels. Here, we show that the phosphatidylinositol 4-phosphate (PI4P)/phosphatidylserine (PS) transfer activity of the endoplasmic reticulum (ER)-resident ORP5 and ORP8 is regulated by both PM PI4P and PI(4,5)P-2. Dynamic control of ORP5/8 recruitment to the PM occurs through interactions with the N-terminal Pleckstrin homology domains and adjacent basic residues of ORP5/8 with both PI4P and PI(4,5)P-2. Although ORP5 activity requires normal levels of these inositides, ORP8 is called on only when PI(4,5) P-2 levels are increased. Regulation of the ORP5/8 attachment to the PM by both phosphoinositides provides a powerful means to determine the relative flux of PI4P toward the ER for PS transport and Sac1-mediated dephosphorylation and PIP 5-kinase-mediated conversion to PI(4,5)P-2. Using this rheostat, cells can maintain PI(4,5)P-2 levels by adjusting the availability of PI4P in the PM.

Název v anglickém jazyce

PI(4,5)P-2 controls plasma membrane PI4P and PS levels via ORP5/8 recruitment to ER-PM contact sites

Popis výsledku anglicky

Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P-2) is a critically important regulatory lipid of the plasma membrane (PM), however, little is known about how cells regulate PM PI(4,5)P-2 levels. Here, we show that the phosphatidylinositol 4-phosphate (PI4P)/phosphatidylserine (PS) transfer activity of the endoplasmic reticulum (ER)-resident ORP5 and ORP8 is regulated by both PM PI4P and PI(4,5)P-2. Dynamic control of ORP5/8 recruitment to the PM occurs through interactions with the N-terminal Pleckstrin homology domains and adjacent basic residues of ORP5/8 with both PI4P and PI(4,5)P-2. Although ORP5 activity requires normal levels of these inositides, ORP8 is called on only when PI(4,5) P-2 levels are increased. Regulation of the ORP5/8 attachment to the PM by both phosphoinositides provides a powerful means to determine the relative flux of PI4P toward the ER for PS transport and Sac1-mediated dephosphorylation and PIP 5-kinase-mediated conversion to PI(4,5)P-2. Using this rheostat, cells can maintain PI(4,5)P-2 levels by adjusting the availability of PI4P in the PM.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA17-05200S" target="_blank" >GA17-05200S: Studium hetoromerických komplexů lipid kinázy PI4KB v roztoku</a><br>

Návaznosti

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

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Journal of Cell Biology

ISSN

0021-9525

e-ISSN

—

Svazek periodika

217

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

17

Strana od-do

1797-1813

Kód UT WoS článku

000431616300021

EID výsledku v databázi Scopus

2-s2.0-85043994614