Phosphorylation of the RSRSP stretch is critical for splicing regulation by RNA-Binding Motif Protein 20 (RBM20) through nuclear localization.

Abstract:

: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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Murayama R,Kimura-Asami M,Togo-Ohno M,Yamasaki-Kato Y,Naruse TK,Yamamoto T,Hayashi T,Ai T,Spoonamore KG,Kovacs RJ,Vatta M,Iizuka M,Saito M,Wani S,Hiraoka Y,Kimura A,Kuroyanagi H

doi

10.1038/s41598-018-26624-w

subject

Has Abstract

pub_date

2018-06-12 00:00:00

pages

8970

issue

1

issn

2045-2322

pii

10.1038/s41598-018-26624-w

journal_volume

8

pub_type

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