MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2014b-1 DIFFERENCES BETWEEN LUTROPIN- AND CHORIOGONADOTROPINMEDIATED RECEPTOR ACTIVATION human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. fcs fluorescence correlation spectroscopy FCS FCS fcs tag fluorescence tag visualisation by fluorescence tag fluorescence gkrause@fmp-Berlin.de 2014 imex curation Grzesik P., Teichmann A., Furkert J., Rutz C., Wiesner B., Kleinau G., Schülein R., Gromoll J., Krause G. FEBS J. (1742-464X) Only protein-protein interactions anonymous-2014b-2 DIFFERENCES BETWEEN LUTROPIN- AND CHORIOGONADOTROPINMEDIATED RECEPTOR ACTIVATION human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. confocal microscopy confocal microscopy tag fluorescence tag visualisation by fluorescence tag fluorescence gkrause@fmp-Berlin.de 2014 imex curation Grzesik P., Teichmann A., Furkert J., Rutz C., Wiesner B., Kleinau G., Schülein R., Gromoll J., Krause G. FEBS J. (1742-464X) Only protein-protein interactions lshr_human Lutropin-choriogonadotropic hormone receptor LHCGR LCGR LGR2 LHRHR Luteinizing hormone receptor protein protein human Homo sapiens Human MKQRFSALQLLKLLLLLQPPLPRALREALCPEPCNCVPDGALRCPGPTAGLTRLSLAYLPVKVIPSQAFRGLNEVIKIEISQIDSLERIEANAFDNLLNLSEILIQNTKNLRYIEPGAFINLPRLKYLSICNTGIRKFPDVTKVFSSESNFILEICDNLHITTIPGNAFQGMNNESVTLKLYGNGFEEVQSHAFNGTTLTSLELKENVHLEKMHNGAFRGATGPKTLDISSTKLQALPSYGLESIQRLIATSSYSLKKLPSRETFVNLLEATLTYPSHCCAFRNLPTKEQNFSHSISENFSKQCESTVRKVNNKTLYSSMLAESELSGWDYEYGFCLPKTPRCAPEPDAFNPCEDIMGYDFLRVLIWLINILAIMGNMTVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKGQYYNHAIDWQTGSGCSTAGFFTVFASELSVYTLTVITLERWHTITYAIHLDQKLRLRHAILIMLGGWLFSSLIAMLPLVGVSNYMKVSICFPMDVETTLSQVYILTILILNVVAFFIICACYIKIYFAVRNPELMATNKDTKIAKKMAILIFTDFTCMAPISFFAISAAFKVPLITVTNSKVLLVLFYPINSCANPFLYAIFTKTFQRDFFLLLSKFGCCKRRAELYRRKDFSAYTSNCKNGFTGSNKPSQSTLKLSTLHCQGTALLDKTRYTEC lhcgr-lhcgr 1477562 n/a hLHR 1477564 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell mcherry tag mcherry mcherry fluorescent protein tag mcherry undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false n/a hLHR 1477564 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell gfp tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false f3 Using fluorescent cross-correlation spectroscopy (FCCS), we tested each co-expressed pair of signaling- and binding-deficient mutants for significant cross-correlation. As a positive control, we used wild type hLHR, and LHR-homodimerization was indeed confirmed in our FCCS experiments. As a negative control, we used a membrane-attached, A kinase anchor protein 18 alpha (AKAP18α-mCherry) construct, co-transfected with hLHR-delExon10. A cross-correlation of 7% was determined, which is consistent with the cross-talk of the systemand indicates that the molecules do not interact. For each pair of deficient mutants, including the hLHR-delExon10, there was significant cross-correlation at the basal cell membrane. Figures 3B and 3C show representative, normalized auto- and cross-correlation curves of GFP, mCherry-tagged receptor constructs hLHR-delExon10, mutant hLHR-C131R, and the negative control with the AKAP18α construct. It was observed that neither the introduced point mutations, such as Cys131Arg and Lys605Glu, nor the complete lack of Exon10 has a significant influence on receptor oligomerization (figure 3A). These results confirm that oligomerization of the hLHRdelExon10 is not disturbed by the lack of the exon10. lhcgr-lhcgr-1 1477563 n/a hLHR 1477564 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell gfp tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false n/a hLHR 1477564 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell mcherry tag mcherry mcherry fluorescent protein tag mcherry undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false colocalization colocalization false false false f3