Gewählte Publikation:
SHR
Neuro
Krebs
Kardio
Lipid
Stoffw
Microb
Schicker, K; Hussl, S; Chandaka, GK; Kosenburger, K; Yang, JW; Waldhoer, M; Sitte, HH; Boehm, S.
A membrane network of receptors and enzymes for adenine nucleotides and nucleosides.
Biochim Biophys Acta. 2009; 1793(2): 325-334.
Doi: 10.1016/j.bbamcr.2008.09.014
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
- Co-Autor*innen der Med Uni Graz
-
Waldhoer Maria
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
- Most cells express more than one receptor plus degrading enzymes for adenine nucleotides or nucleosides, and cellular responses to purines are rarely compatible with the actions of single receptors. Therefore, these receptors are viewed as components of a combinatorial receptor web rather than self-dependent entities, but it remained unclear to what extent they can associate with each other to form signalling units. P2Y(1), P2Y(2), P2Y(12), P2Y(13), P2X(2), A(1), A(2A) receptors and NTPDase1 and -2 were expressed as fluorescent fusion proteins which were targeted to membranes and signalled like the unlabelled counterparts. When tested by FRET microscopy, all the G protein-coupled receptors proved able to form heterooligomers with each other, and P2Y(1), P2Y(12), P2Y(13), A(1), A(2A), and P2X(2) receptors also formed homooligomers. P2Y receptors did not associate with P2X, but G protein-coupled receptors formed heterooligomers with NTPDase1, but not NTPDase2. The specificity of prototypic interactions (P2Y(1)/P2Y(1), A(2A)/P2Y(1), A(2A)/P2Y(12)) was corroborated by FRET competition or co-immunoprecipitation. These results demonstrate that G protein-coupled purine receptors associate with each other and with NTPDase1 in a highly promiscuous manner. Thus, purinergic signalling is not only determined by the expression of receptors and enzymes but also by their direct interaction within a previously unrecognized multifarious membrane network.
- Find related publications in this database (using NLM MeSH Indexing)
-
Adenine Nucleotides - metabolism
-
Adenosine Diphosphate - metabolism
-
Adenosine Triphosphate - metabolism
-
Animals -
-
Antigens, CD - metabolism
-
Apyrase - metabolism
-
Cell Line -
-
Cell Membrane - enzymology
-
Fluorescence -
-
Fluorescence Resonance Energy Transfer -
-
Humans -
-
Hydrolysis -
-
Immunoprecipitation -
-
Membrane Potentials -
-
Mice -
-
Nucleosides - metabolism
-
Protein Binding -
-
Protein Subunits - metabolism
-
Rats -
-
Receptors, G-Protein-Coupled - metabolism
-
Receptors, Purinergic - metabolism
-
Recombinant Fusion Proteins - metabolism
-
Reproducibility of Results -
- Find related publications in this database (Keywords)
-
Adenosine receptor
-
P2Y receptor
-
P2X receptor
-
NTPDase
-
FRET