@article{oai:nagoya.repo.nii.ac.jp:00008799, author = {INOUE, MASAHIKO and WAKAYAMA, YOSHIHIRO and JIMI, TAKAHIRO and SHIBUYA, SEIJI and HARA, HAJIME and UNAKI, AKIHIKO and KENMOCHI, KIYOKAZU}, issue = {3-4}, journal = {Nagoya Journal of Medical Science}, month = {Aug}, note = {Syntrophins are the cytoplasmic peripheral proteins of dystrophin glycoprotein complex, of which five (α1, β1, β2, γ1 and γ2) isoforms have been identified so far. Respective syntrophin isoforms are encoded by different genes but have similar domain structures. At the sarcolemma of skeletal muscle, the most abundant α1-syntrophin was shown to interact at its PDZ domain with many membrane proteins. Among them, the AQP4 interaction with α1-syntrophin PDZ domain was demonstrated by a Tg mouse study, prompting us to investigate the interaction between mouse α1-syntrophin (BC018546: nt.267–492, PDZ domain) pEXP-AD502 as prey vector and mouse AQP4 (NM009700: nt.805–969) pDBLeu as bait vector by the yeast two-hybrid assay, resulting in a negative study. We further studied the binding partner of another sarcolemma located β1-syntrophin, and performed a yeast two-hybrid experiment. With human β1-syntrophin as bait and human skeletal muscle cDNA library as prey, we obtained one positive clone which turned out to be α-dystrobrevin. Although the interaction of human β1-syntrophin with α-dystrobrevin has already been shown by immunoprecipitation assay, we have here confirmed this interaction by a yeast two-hybrid experiment.}, pages = {117--126}, title = {SKELETAL MUSCLE SYNTROPHIN INTERACTORS REVEALED BY YEAST TWO-HYBRID ASSAY}, volume = {70}, year = {2008} }