Functional Coupling of NKR-P1 Receptors to Various Heterotrimeric G Proteins in Rat Interleukin-2-activated Natural Killer Cells *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 272, Issue: 50, Page: 31604-31608
1997
- 15Citations
- 6Captures
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Metrics Details
- Citations15
- Citation Indexes15
- 15
- CrossRef14
- Captures6
- Readers6
Article Description
NKR-P1 molecules constitute a family of type II membrane receptors in natural killer (NK) cells that preferentially activate NK cell killing and release of interferon-γ from these cells. Here, we demonstrate that anti-NKR-P1 enhances GTP binding in rat interleukin-2-activated NK cell membranes; GTP binding to G i3 α, G s α, G q,11 α, and G z α increased noticeably in these cell membranes after treatment with anti-NKR-P1. Western blot analysis of membrane proteins prepared from interleukin-2-activated NK cells reveals the presence of G i1,2 α, G i3 α, G o α, G s α, G q,11 α, G z α, and G 12 α, but not G 13 α. However, only α i3, α s, α q,11, and α z, but not α i1,2, α o, α 12, or α 13 subunits when immunoprecipitated with the appropriate anti-G protein antibodies, are associated with NKR-P1 when immunoblotted with anti-NKR-P1. Reciprocally, NKR-P1 immunoprecipitated with anti-NKR-P1 is associated with α i3, α s, α q,11, and α z immunoblotted with anti-G proteins. These results are the first to demonstrate the physical and functional coupling of NKR-P1 to the heterotrimeric G proteins in NK cells.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S002192581988794X; http://dx.doi.org/10.1074/jbc.272.50.31604; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0031468587&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9395499; https://linkinghub.elsevier.com/retrieve/pii/S002192581988794X; https://dx.doi.org/10.1074/jbc.272.50.31604
Elsevier BV
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