Phosphatidylinositol 4-kinase III beta (PI4KB) forms highly flexible heterocomplexes that include ACBD3, 14-3-3, and Rab11 proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00501576" target="_blank" >RIV/61388963:_____/19:00501576 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.nature.com/articles/s41598-018-37158-6" target="_blank" >https://www.nature.com/articles/s41598-018-37158-6</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-018-37158-6" target="_blank" >10.1038/s41598-018-37158-6</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Phosphatidylinositol 4-kinase III beta (PI4KB) forms highly flexible heterocomplexes that include ACBD3, 14-3-3, and Rab11 proteins

Popis výsledku v původním jazyce

Phosphatidylinositol 4-kinase III beta (PI4KB) is a key enzyme of the Golgi system because it produces its lipid hallmark the phosphatidylinositol 4-phosphate (PI4P). It is recruited to Golgi by the Golgi resident ACBD3 protein, regulated by 14-3-3 proteins and it also serves as an adaptor because it recruits the small GTPase Rab11. Here, we analyzed the protein complexes formed by PI4KB in vitro using small angle x-ray scattering (SAXS) and we discovered that these protein complexes are highly flexible. The 14-3-3:PI4KB:Rab11 protein complex has 2:1:1 stoichiometry and its different conformations are rather compact, however, the ACBD3:PI4KB protein complex has both, very compact and very extended conformations. Furthermore, in vitro reconstitution revealed that the membrane is necessary for the formation of ACBD3:PI4KB:Rab11 protein complex at physiological (nanomolar) concentrations.

Název v anglickém jazyce

Phosphatidylinositol 4-kinase III beta (PI4KB) forms highly flexible heterocomplexes that include ACBD3, 14-3-3, and Rab11 proteins

Popis výsledku anglicky

Phosphatidylinositol 4-kinase III beta (PI4KB) is a key enzyme of the Golgi system because it produces its lipid hallmark the phosphatidylinositol 4-phosphate (PI4P). It is recruited to Golgi by the Golgi resident ACBD3 protein, regulated by 14-3-3 proteins and it also serves as an adaptor because it recruits the small GTPase Rab11. Here, we analyzed the protein complexes formed by PI4KB in vitro using small angle x-ray scattering (SAXS) and we discovered that these protein complexes are highly flexible. The 14-3-3:PI4KB:Rab11 protein complex has 2:1:1 stoichiometry and its different conformations are rather compact, however, the ACBD3:PI4KB protein complex has both, very compact and very extended conformations. Furthermore, in vitro reconstitution revealed that the membrane is necessary for the formation of ACBD3:PI4KB:Rab11 protein complex at physiological (nanomolar) concentrations.

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

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

Scientific Reports

ISSN

2045-2322

e-ISSN

—

Svazek periodika

9

Číslo periodika v rámci svazku

Jan 24

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

567

Kód UT WoS článku

000456554600006

EID výsledku v databázi Scopus

2-s2.0-85060556364