MBNL1 associates with YB-1 in cytoplasmic stress granules

Hayato Onishi, Yoshihiro Kino, Tomoko Morita, Eugene Futai, Noboru Sasagawa, Shoichi Ishiura

研究成果: Article査読

55 被引用数 (Scopus)

抄録

The muscleblind-like (MBNL) protein family is thought to be involved in the molecular mechanism of myotonic dystrophy (DM). Although it has been shown to have splicing activity, a broader function in cellular RNA metabolism has been implicated. In this study, we attempted to find the binding proteins of MBNL1 in order to elucidate its physiological function. First, we performed a GST pull-down assay using GST-MBNL1-6xHis as bait. Several proteins were identified, including YB-1, a multifunctional DNA/RNA-binding protein, and DDX1, a DEAD box RNA helicase. MBNL1 formed an RNP complex with YB-1 and DDX1 in binding assays. YB-1 also showed a weak but significant effect on α-actinin splice site selection. Interestingly, in response to stress, MBNL1 moved to cytoplasmic stress granules, where it colocalized with YB-1, which was previously reported to be a component of stress granules. We found that DDX1 also colocalized with MBNL1 at stress granules. These results provide new insight into the dynamics of MBNL1 in response to stress, and they suggest a role for MBNL1 in mRNA metabolism in the cytoplasm.

本文言語English
ページ(範囲)1994-2002
ページ数9
ジャーナルJournal of Neuroscience Research
86
9
DOI
出版ステータスPublished - 2008 7 1
外部発表はい

ASJC Scopus subject areas

  • 細胞および分子神経科学

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