Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00459191" target="_blank" >RIV/61388971:_____/16:00459191 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/16:00459191 RIV/00216208:11310/16:10324227

Result on the web

<a href="http://www.nature.com/articles/srep23641" target="_blank" >http://www.nature.com/articles/srep23641</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/srep23641" target="_blank" >10.1038/srep23641</a>

Result language

angličtina

Original language name

Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein

Original language description

Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells. To convert their lipid substrates, PI4Ks must be recruited to the correct membrane compartment. PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown. Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3). We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

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

Name of the periodical

Scientific Reports

ISSN

2045-2322

e-ISSN

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Volume of the periodical

6

Issue of the periodical within the volume

Mar 24

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

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UT code for WoS article

000372699800001

EID of the result in the Scopus database

2-s2.0-84961637073