Distinct specificity in the binding of inositol phosphates by pleckstrin homology domains of pleckstrin, RAC-protein kinase, diacylglycerol kinase and a new 130 kDa protein

Hiroshi Takeuchi, Takashi Kanematsu, Yoshio Misumi, Fumio Sakane, Hiroaki Konishi, Ushio Kikkawa, Yutaka Watanabe, Matilda Katan, Masato Hirata

研究成果: ジャーナルへの寄稿学術誌査読

90 被引用数 (Scopus)

抄録

The pleckstrin homology domains (PH domains) derived from four different proteins, the N-terminal part of pleckstrin, RAC-protein kinase, diacylglycerol kinase and the 130 kDa protein originally cloned as an inositol 1,4,5-trisphosphate binding protein, were analysed for binding of inositol phosphates and derivatives of inositol lipids. The PH domain from pleckstrin bound inositol phosphates according to a number of phosphates on the inositol ring, i.e. more phosphate groups, stronger the binding, but a very limited specificity due to the 2-phosphate was also observed. On the other hand, the PH domain from RAC-protein kinase and diacylglycerol kinase specifically bound inositol 1,3,4,5,6-pentakisphosphate and inositol 1,4,5,6- tetrakisphosphate most strongly. The PH domain from the 130 kDa protein, however, had a preference for inositol 1,4,5-trisphosphate and 1,4,5,6- tetrakisphosphate. Comparison was also made between binding of inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate and soluble derivatives of their corresponding phospholipids. The PH domains examined, except that from pleckstrin, showed a 8- to 42-times higher affinity for inositol 1,4,5-trisphosphate than that for corresponding phosphonoisitide derivative. However, all PH domains had similar affinity inositol 1,3,4,5- tetrakisphosphate compared to the corresponding lipid derivative. The present study supports our previous proposal that inositol phosphates and/or inositol lipids could be important lipids could be important ligands for the PH domain, and therefore inositol phosphate/inositol lipids may have the considerable versatility in the control of diverse cellular function. Which of these potential ligands are physiologically relevant would depend on the binding affinities and their cellular abundance.

本文言語英語
ページ(範囲)275-285
ページ数11
ジャーナルBiochimica et Biophysica Acta - Molecular Cell Research
1359
3
DOI
出版ステータス出版済み - 12月 12 1997

!!!All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 細胞生物学

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