-
Je něco špatně v tomto záznamu ?
Phosphatidylinositol 4-kinase IIIβ (PI4KB) forms highly flexible heterocomplexes that include ACBD3, 14-3-3, and Rab11 proteins
D. Chalupska, B. Różycki, J. Humpolickova, L. Faltova, M. Klima, E. Boura,
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Directory of Open Access Journals
od 2011
Free Medical Journals
od 2011
Nature Open Access
od 2011-12-01
PubMed Central
od 2011
Europe PubMed Central
od 2011
ProQuest Central
od 2011-01-01
Open Access Digital Library
od 2011-01-01
Open Access Digital Library
od 2011-01-01
Health & Medicine (ProQuest)
od 2011-01-01
ROAD: Directory of Open Access Scholarly Resources
od 2011
Springer Nature OA/Free Journals
od 2011-12-01
- MeSH
- adaptorové proteiny signální transdukční metabolismus MeSH
- fosfotransferasy s alkoholovou skupinou jako akceptorem metabolismus MeSH
- intracelulární membrány metabolismus MeSH
- maloúhlový rozptyl MeSH
- membránové proteiny metabolismus MeSH
- multimerizace proteinu * MeSH
- proteiny 14-3-3 metabolismus MeSH
- rab proteiny vázající GTP metabolismus MeSH
- rekombinantní proteiny metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Phosphatidylinositol 4-kinase IIIβ (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.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc20025956
- 003
- CZ-PrNML
- 005
- 20201222154227.0
- 007
- ta
- 008
- 201125s2019 xxk f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1038/s41598-018-37158-6 $2 doi
- 035 __
- $a (PubMed)30679637
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxk
- 100 1_
- $a Chalupska, Dominika $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nam. 2., Prague, Czech Republic.
- 245 10
- $a Phosphatidylinositol 4-kinase IIIβ (PI4KB) forms highly flexible heterocomplexes that include ACBD3, 14-3-3, and Rab11 proteins / $c D. Chalupska, B. Różycki, J. Humpolickova, L. Faltova, M. Klima, E. Boura,
- 520 9_
- $a Phosphatidylinositol 4-kinase IIIβ (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.
- 650 _2
- $a proteiny 14-3-3 $x metabolismus $7 D048948
- 650 _2
- $a adaptorové proteiny signální transdukční $x metabolismus $7 D048868
- 650 _2
- $a intracelulární membrány $x metabolismus $7 D007425
- 650 _2
- $a membránové proteiny $x metabolismus $7 D008565
- 650 _2
- $a fosfotransferasy s alkoholovou skupinou jako akceptorem $x metabolismus $7 D017853
- 650 12
- $a multimerizace proteinu $7 D055503
- 650 _2
- $a rekombinantní proteiny $x metabolismus $7 D011994
- 650 _2
- $a maloúhlový rozptyl $7 D053838
- 650 _2
- $a rab proteiny vázající GTP $x metabolismus $7 D020691
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Różycki, Bartosz $u Institute of Physics, Polish Academy of Sciences, Al. Lotnikow 32/46, 02-668, Warsaw, Poland.
- 700 1_
- $a Humpolickova, Jana $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nam. 2., Prague, Czech Republic.
- 700 1_
- $a Faltova, Lenka $u Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institute, 5232, Villigen, PSI, Switzerland.
- 700 1_
- $a Klima, Martin $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nam. 2., Prague, Czech Republic.
- 700 1_
- $a Boura, Evzen $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nam. 2., Prague, Czech Republic. boura@uochb.cas.cz.
- 773 0_
- $w MED00182195 $t Scientific reports $x 2045-2322 $g Roč. 9, č. 1 (2019), s. 567
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/30679637 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20201125 $b ABA008
- 991 __
- $a 20201222154223 $b ABA008
- 999 __
- $a ok $b bmc $g 1600101 $s 1116642
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2019 $b 9 $c 1 $d 567 $e 20190124 $i 2045-2322 $m Scientific reports $n Sci Rep $x MED00182195
- LZP __
- $a Pubmed-20201125