Detail
Article
Online article
FT
Medvik - BMC
  • Something wrong with this record ?

Kappa but not delta or mu opioid receptors form homodimers at low membrane densities

K. Cechova, C. Lan, M. Macik, NPF. Barthes, M. Jung, MH. Ulbrich

. 2021 ; 78 (23) : 7557-7568. [pub] 20211017

Language English Country Switzerland

Document type Journal Article

Grant support
UL 312/6-1 deutsche forschungsgemeinschaft
RTG 2202 deutsche forschungsgemeinschaft
EXC 294 deutsche forschungsgemeinschaft
CRC 992 deutsche forschungsgemeinschaft
EXC-2189-Project ID: 390939984 deutsche forschungsgemeinschaft
GA17-05903S grantová agentura české republiky
SVV260427/2020 univerzita karlova v praze
FM/a/2017-2-072 univerzita karlova v praze
SVV260427/2018 univerzita karlova v praze

E-resources Online Full text

NLK PubMed Central from 1997
ProQuest Central from 1997-01-01 to 1 year ago
Medline Complete (EBSCOhost) from 2000-01-01 to 1 year ago
Health & Medicine (ProQuest) from 1997-01-01 to 1 year ago

Opioid receptors (ORs) have been observed as homo- and heterodimers, but it is unclear if the dimers are stable under physiological conditions, and whether monomers or dimers comprise the predominant fraction in a cell. Here, we use three live-cell imaging approaches to assess dimerization of ORs at expression levels that are 10-100 × smaller than in classical biochemical assays. At membrane densities around 25/µm2, a split-GFP assay reveals that κOR dimerizes, while µOR and δOR stay monomeric. At receptor densities < 5/µm2, single-molecule imaging showed no κOR dimers, supporting the concept that dimer formation depends on receptor membrane density. To directly observe the transition from monomers to dimers, we used a single-molecule assay to assess membrane protein interactions at densities up to 100 × higher than conventional single-molecule imaging. We observe that κOR is monomeric at densities < 10/µm2 and forms dimers at densities that are considered physiological. In contrast, µOR and δOR stay monomeric even at the highest densities covered by our approach. The observation of long-lasting co-localization of red and green κOR spots suggests that it is a specific effect based on OR dimerization and not an artefact of coincidental encounters.

References provided by Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc22003062
003      
CZ-PrNML
005      
20220127150710.0
007      
ta
008      
220113s2021 sz f 000 0|eng||
009      
AR
024    7_
$a 10.1007/s00018-021-03963-y $2 doi
035    __
$a (PubMed)34657173
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a sz
100    1_
$a Cechova, Kristina $u Department of Biomathematics, Institute of Physiology, Czech Academy of Sciences, Prague, Czech Republic $u Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic
245    10
$a Kappa but not delta or mu opioid receptors form homodimers at low membrane densities / $c K. Cechova, C. Lan, M. Macik, NPF. Barthes, M. Jung, MH. Ulbrich
520    9_
$a Opioid receptors (ORs) have been observed as homo- and heterodimers, but it is unclear if the dimers are stable under physiological conditions, and whether monomers or dimers comprise the predominant fraction in a cell. Here, we use three live-cell imaging approaches to assess dimerization of ORs at expression levels that are 10-100 × smaller than in classical biochemical assays. At membrane densities around 25/µm2, a split-GFP assay reveals that κOR dimerizes, while µOR and δOR stay monomeric. At receptor densities < 5/µm2, single-molecule imaging showed no κOR dimers, supporting the concept that dimer formation depends on receptor membrane density. To directly observe the transition from monomers to dimers, we used a single-molecule assay to assess membrane protein interactions at densities up to 100 × higher than conventional single-molecule imaging. We observe that κOR is monomeric at densities < 10/µm2 and forms dimers at densities that are considered physiological. In contrast, µOR and δOR stay monomeric even at the highest densities covered by our approach. The observation of long-lasting co-localization of red and green κOR spots suggests that it is a specific effect based on OR dimerization and not an artefact of coincidental encounters.
650    _2
$a zvířata $7 D000818
650    _2
$a buněčná membrána $x metabolismus $7 D002462
650    _2
$a myši $7 D051379
650    _2
$a konformace proteinů $7 D011487
650    _2
$a multimerizace proteinu $7 D055503
650    _2
$a krysa rodu Rattus $7 D051381
650    _2
$a receptory opiátové delta $x chemie $x metabolismus $7 D017465
650    _2
$a receptory opiátové mu $x chemie $x metabolismus $7 D017450
650    _2
$a zobrazení jednotlivé molekuly $x metody $7 D000072760
650    _2
$a analýza jednotlivých buněk $x metody $7 D059010
655    _2
$a časopisecké články $7 D016428
700    1_
$a Lan, Chenyang $u Faculty of Biology, University of Freiburg, Freiburg, Germany
700    1_
$a Macik, Matus $u , Prague, Czech Republic
700    1_
$a Barthes, Nicolas P F $u Institute of Pharmaceutical Sciences, University of Freiburg, Freiburg, Germany
700    1_
$a Jung, Manfred $u Institute of Pharmaceutical Sciences, University of Freiburg, Freiburg, Germany $u CIBSS-Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany
700    1_
$a Ulbrich, Maximilian H $u Institute of Internal Medicine IV, Medical Center of the University of Freiburg, Freiburg, Germany. max.ulbrich@bioss.uni-freiburg.de $u BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany. max.ulbrich@bioss.uni-freiburg.de
773    0_
$w MED00001078 $t Cellular and molecular life sciences : CMLS $x 1420-9071 $g Roč. 78, č. 23 (2021), s. 7557-7568
856    41
$u https://pubmed.ncbi.nlm.nih.gov/34657173 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y p $z 0
990    __
$a 20220113 $b ABA008
991    __
$a 20220127150706 $b ABA008
999    __
$a ok $b bmc $g 1750743 $s 1154211
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2021 $b 78 $c 23 $d 7557-7568 $e 20211017 $i 1420-9071 $m Cellular and molecular life sciences $n Cell Mol Life Sci $x MED00001078
GRA    __
$a UL 312/6-1 $p deutsche forschungsgemeinschaft
GRA    __
$a RTG 2202 $p deutsche forschungsgemeinschaft
GRA    __
$a EXC 294 $p deutsche forschungsgemeinschaft
GRA    __
$a CRC 992 $p deutsche forschungsgemeinschaft
GRA    __
$a EXC-2189-Project ID: 390939984 $p deutsche forschungsgemeinschaft
GRA    __
$a GA17-05903S $p grantová agentura české republiky
GRA    __
$a SVV260427/2020 $p univerzita karlova v praze
GRA    __
$a FM/a/2017-2-072 $p univerzita karlova v praze
GRA    __
$a SVV260427/2018 $p univerzita karlova v praze
LZP    __
$a Pubmed-20220113

Find record

Citation metrics

Loading data ...

Archiving options

Loading data ...