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Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells
L. Adámková, Z. Kvíčalová, D. Rozbeský, Z. Kukačka, D. Adámek, M. Cebecauer, P. Novák,
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články
Grantová podpora
16-24309S
Grantová Agentura České Republiky
LH15010
Ministry of Education of the Czech Republic
LD15089
Ministry of Education of the Czech Republic
LQ1604
Ministry of Education of the Czech Republic
RVO61388971
Akademie Věd České Republiky
L200201801
Akademie Věd České Republiky
260443
Univerzita Karlova v Praze
CZ.1.05/1.1.00/02.0109 BIOCEV
European Regional Development Fund
LM2015043 CIISB for CMS BIOCEV
Ministry of Education of the Czech Republic
NLK
Free Medical Journals
od 2000
Freely Accessible Science Journals
od 2000
PubMed Central
od 2007
Europe PubMed Central
od 2007
ProQuest Central
od 2000-03-01
Open Access Digital Library
od 2000-01-01
Open Access Digital Library
od 2007-01-01
Health & Medicine (ProQuest)
od 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
od 2000
PubMed
30995786
DOI
10.3390/ijms20081884
Knihovny.cz E-zdroje
- MeSH
- antigeny Ly analýza MeSH
- Cercopithecus aethiops MeSH
- COS buňky MeSH
- Jurkat buňky MeSH
- lektinové receptory NK-buněk - podrodina B analýza MeSH
- lidé MeSH
- multimerizace proteinu MeSH
- myši inbrední C57BL MeSH
- myši MeSH
- receptory imunologické analýza MeSH
- refolding proteinů MeSH
- rezonanční přenos fluorescenční energie MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
Mouse activating Nkrp1 proteins are commonly described as type II transmembrane receptors with disulfide-linked homodimeric structure. Their function and the manner in which Nkrp1 proteins of mouse strain (C57BL/6) oligomerize are still poorly understood. To assess the oligomerization state of Nkrp1 proteins, mouse activating EGFP-Nkrp1s were expressed in mammalian lymphoid cells and their oligomerization evaluated by Förster resonance energy transfer (FRET). Alternatively, Nkrp1s oligomers were detected by Western blotting to specify the ratio between monomeric and dimeric forms. We also performed structural characterization of recombinant ectodomains of activating Nkrp1 receptors. Nkrp1 isoforms c1, c2 and f were expressed prevalently as homodimers, whereas the Nkrp1a displays larger proportion of monomers on the cell surface. Cysteine-to-serine mutants revealed the importance of all stalk cysteines for protein dimerization in living cells with a major influence of cysteine at position 74 in two Nkrp1 protein isoforms. Our results represent a new insight into the oligomerization of Nkrp1 receptors on lymphoid cells, which will help to determine their function.
Citace poskytuje Crossref.org
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- $a Adámková, Ljubina $u Laboratory of Structural Biology and Cell Signaling, Institute of Microbiology, The Czech Academy of Sciences, Vídeňská 1083, 14220 Prague 4, Czech Republic. ljubina.adamkova@biomed.cas.cz.
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- $a Mouse activating Nkrp1 proteins are commonly described as type II transmembrane receptors with disulfide-linked homodimeric structure. Their function and the manner in which Nkrp1 proteins of mouse strain (C57BL/6) oligomerize are still poorly understood. To assess the oligomerization state of Nkrp1 proteins, mouse activating EGFP-Nkrp1s were expressed in mammalian lymphoid cells and their oligomerization evaluated by Förster resonance energy transfer (FRET). Alternatively, Nkrp1s oligomers were detected by Western blotting to specify the ratio between monomeric and dimeric forms. We also performed structural characterization of recombinant ectodomains of activating Nkrp1 receptors. Nkrp1 isoforms c1, c2 and f were expressed prevalently as homodimers, whereas the Nkrp1a displays larger proportion of monomers on the cell surface. Cysteine-to-serine mutants revealed the importance of all stalk cysteines for protein dimerization in living cells with a major influence of cysteine at position 74 in two Nkrp1 protein isoforms. Our results represent a new insight into the oligomerization of Nkrp1 receptors on lymphoid cells, which will help to determine their function.
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- $a Cebecauer, Marek $u Department of Biophysical Chemistry, J. Heyrovsky Institute of Physical Chemistry, The Czech Academy of Sciences, Dolejškova 2155/3, 18223 Prague 8, Czech Republic. marek.cebecauer@jh-inst.cas.cz.
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- $a Novák, Petr $u Laboratory of Structural Biology and Cell Signaling, Institute of Microbiology, The Czech Academy of Sciences, Vídeňská 1083, 14220 Prague 4, Czech Republic. pnovak@biomed.cas.cz. Department of Biochemistry, Charles University, Hlavova 8, 12843 Prague 2, Czech Republic. pnovak@biomed.cas.cz.
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