論文

査読有り
2017年4月

Splicing variation of Long-IRBIT determines the target selectivity of IRBIT family proteins

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
  • Katsuhiro Kawaai
  • ,
  • Hideaki Ando
  • ,
  • Nobuhiko Satoh
  • ,
  • Hideomi Yamada
  • ,
  • Naoko Ogawa
  • ,
  • Matsumi Hirose
  • ,
  • Akihiro Mizutani
  • ,
  • Benjamin Bonneau
  • ,
  • George Seki
  • ,
  • Katsuhiko Mikoshiba

114
15
開始ページ
3921
終了ページ
3926
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1073/pnas.1618514114
出版者・発行元
NATL ACAD SCIENCES

IRBIT [inositol 1,4,5-trisphosphate receptor (IP3R) binding protein released with inositol 1,4,5-trisphosphate (IP3)] is a multifunctional protein that regulates several target molecules such as ion channels, transporters, polyadenylation complex, and kinases. Through its interaction with multiple targets, IRBIT contributes to calcium signaling, electrolyte transport, mRNA processing, cell cycle, and neuronal function. However, the regulatory mechanism of IRBIT binding to particular targets is poorly understood. Long-IRBIT is an IRBIT homolog with high homology to IRBIT, except for a unique N-terminal appendage. Long-IRBIT splice variants have different N-terminal sequences and a common C-terminal region, which is involved in multimerization of IRBIT and Long-IRBIT. In this study, we characterized IRBIT and Long-IRBIT splice variants (IRBIT family). We determined that the IRBIT family exhibits different mRNA expression patterns in various tissues. The IRBIT family formed homo-and heteromultimers. In addition, N-terminal splicing of Long-IRBIT changed the protein stability and selectivity to target molecules. These results suggest that N-terminal diversity of the IRBIT family and various combinations of multimer formation contribute to the functional diversity of the IRBIT family.

Web of Science ® 被引用回数 : 6

リンク情報
DOI
https://doi.org/10.1073/pnas.1618514114
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000398789800049&DestApp=WOS_CPL

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