Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep44870
Title: Stk38 Modulates Rbm24 Protein Stability to Regulate Sarcomere Assembly in Cardiomyocytes
Authors: Liu, J
Kong, X
Yew Mun, L 
Meng Kai, Z
Li Yan, G
Lin, Y
Lim, T.K 
Lin, Q 
Xu, X.Q
Keywords: cell cycle protein
N-myc downstream-regulated gene 1 protein
Rbm24 protein, mouse
RNA binding protein
signal peptide
animal
C57BL mouse
cardiac muscle cell
cell line
immunoprecipitation
mass spectrometry
metabolism
phosphorylation
physiology
protein processing
protein stability
sarcomere
Animals
Cell Cycle Proteins
Cell Line
Immunoprecipitation
Intracellular Signaling Peptides and Proteins
Mass Spectrometry
Mice, Inbred C57BL
Myocytes, Cardiac
Phosphorylation
Protein Processing, Post-Translational
Protein Stability
RNA-Binding Proteins
Sarcomeres
Issue Date: 2017
Citation: Liu, J, Kong, X, Yew Mun, L, Meng Kai, Z, Li Yan, G, Lin, Y, Lim, T.K, Lin, Q, Xu, X.Q (2017). Stk38 Modulates Rbm24 Protein Stability to Regulate Sarcomere Assembly in Cardiomyocytes. Scientific Reports 7 : 44870. ScholarBank@NUS Repository. https://doi.org/10.1038/srep44870
Abstract: RNA-binding protein Rbm24 is a key regulator of heart development and required for sarcomere assembly and heart contractility. Yet, its underlying mechanism remains unclear. Here, we link serine/threonine kinase 38 (Stk38) signaling to the regulation of Rbm24 by showing that Rbm24 phosphorylation and its function could be modulated by Stk38. Using co-immunoprecipitation coupled with mass spectrometry technique, we identified Stk38 as an endogenous binding partner of Rbm24. Stk38 knockdown resulted in decreased Rbm24 protein level in cardiomyocytes. Further studies using Stk38 kinase inhibitor or activator showed that Rbm24 protein stability was regulated in a kinase activity-dependent manner. Deficiency of Stk38 caused reduction of sarcomere proteins and disarrangement of sarcomere, suggesting that Stk38 is essential for Rbm24 to regulate sarcomere assembly. Our results revealed that Stk38 kinase catalyzes the phosphorylation of Rbm24 during sarcomerogensis and this orchestrates accurate sarcomere alignment. This furthers our understanding of the regulatory mechanism of cardiac sarcomere assembly in both physiologic and pathologic contexts, and uncovers a potential novel pathway to cardiomyopathy through modulating the Stk38/Rbm24 protein activity. © 2017 The Author(s).
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/173931
ISSN: 20452322
DOI: 10.1038/srep44870
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