Number of the records: 1
Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein
- 1.
SYSNO ASEP 0459191 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein Author(s) Klíma, Martin (UOCHB-X) RID, ORCID
Tóth, D. J. (US)
Hexnerová, Rozálie (UOCHB-X) ORCID, RID
Bäumlová, Adriana (UOCHB-X)
Chalupská, Dominika (UOCHB-X) ORCID
Tykvart, Jan (UOCHB-X) RID, ORCID
Řežábková, L. (CH)
Sengupta, N. (US)
Man, Petr (MBU-M) RID, ORCID
Dubánková, Anna (UOCHB-X)
Humpolíčková, Jana (UOCHB-X) ORCID
Nencka, Radim (UOCHB-X) RID, ORCID
Veverka, Václav (UOCHB-X) RID, ORCID
Balla, T. (US)
Bouřa, Evžen (UOCHB-X) ORCIDArticle number 23641 Source Title Scientific Reports. - : Nature Publishing Group - ISSN 2045-2322
Roč. 6, Mar 24 (2016)Number of pages 11 s. Language eng - English Country GB - United Kingdom Keywords 4-kinase III beta ; phosphatidylinositol 4-kinases ; endoplasmic reticulum Subject RIV CE - Biochemistry Subject RIV - cooperation Institute of Microbiology - Microbiology, Virology R&D Projects GJ15-21030Y GA ČR - Czech Science Foundation (CSF) LO1302 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LK11205 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LO1304 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LO1509 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support UOCHB-X - RVO:61388963 ; MBU-M - RVO:61388971 UT WOS 000372699800001 EID SCOPUS 84961637073 DOI https://doi.org/10.1038/srep23641 Annotation 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. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2017 Electronic address http://www.nature.com/articles/srep23641
Number of the records: 1