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Detection of Inositol Phosphates by Split PH Domains

  • Reiko Sakaguchi
  • Shunsuke Tajima
  • Yasuo Mori
  • Takashi MoriiEmail author
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 2091)

Abstract

The pleckstrin homology (PH) domain is a family of structurally conserved proteins which can bind inositol phosphate derivatives. Some proteins involved in cellular signaling and cytoskeletal organization possess split PH domains that assemble into a structure which can bind specific inositol phosphates. Here we describe the design of split PH domain from a structurally well-characterized PH domain of phospholipase C (PLC) δ1 and Bruton’s tyrosine kinase (Btk), which selectively bind Ins(1,4,5)P3 and Ins(1,3,4,5)P4, respectively. The PH domains fold into a functional structure when the split halves are brought to close proximity, and can be utilized to detect specific inositol phosphate of interest.

Key words

Inositol phosphates PH domain Structure-based design Fluorescence 

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2020

Authors and Affiliations

  • Reiko Sakaguchi
    • 1
  • Shunsuke Tajima
    • 2
  • Yasuo Mori
    • 1
    • 3
  • Takashi Morii
    • 2
    Email author
  1. 1.Institute for Integrated Cell-Material SciencesKyoto UniversityNishikyo-kuJapan
  2. 2.Institute of Advanced EnergyKyoto UniversityUjiJapan
  3. 3.Department of Synthetic Chemistry and Biological Chemistry, Graduate School of EngineeringKyoto UniversityNishikyo-kuJapan

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