@article{oai:u-ryukyu.repo.nii.ac.jp:02011538,
 author = {Murayama, Rie and Kimura-Asami, Mariko and Togo-Ohno, Marina and Yamasaki-Kato, Yumiko and Naruse, Taeko K. and Yamamoto, Takeshi and Hayashi, Takeharu and Ai, Tomohiko and Spoonamore, Katherine G. and Kovacs, Richard J. and Vatta, Matteo and Iizuka, Mai and Saito, Masumi and Wani, Shotaro and Hiraoka, Yuichi and Kimura, Akinori and Kuroyanagi, Hidehito},
 journal = {Scientific Reports},
 month = {Jul},
 note = {RBM20 is a major regulator of heart-specific alternative pre-mRNA splicing of TTN encoding a giant sarcomeric protein titin. Mutation in RBM20 is linked to autosomal-dominant familial dilated cardiomyopathy (DCM), yet most of the RBM20 missense mutations in familial and sporadic cases were mapped to an RSRSP stretch in an arginine/serine-rich region of which function remains unknown. In the present study, we identified an R634W missense mutation within the stretch and a G1031X nonsense mutation in cohorts of DCM patients. We demonstrate that the two serine residues in the RSRSP stretch are constitutively phosphorylated and mutations in the stretch disturb nuclear localization of RBM20. Rbm20^<S637A> knock-in mouse mimicking an S635A mutation reported in a familial case showed a remarkable effect on titin isoform expression like in a patient carrying the mutation. These results revealed the function of the RSRSP stretch as a critical part of a nuclear localization signal and offer the Rbm20^<S637A> mouse as a good model for in vivo study., 論文},
 title = {Phosphorylation of the RSRSP stretch is critical for splicing regulation by RNA-Binding Motif Protein 20 (RBM20) through nuclear localization},
 volume = {8},
 year = {2018}
}