A target of phosphatidylinositol 3,4,5-trisphosphate with a zinc finger motif similar to that of the ADP-ribosylation-factor GTPase-activating protein and two pleckstrin homology domains

Kenichi Tanaka, Shinobu Imajoh-Ohmi, Takayuki Sawada, Ryuichi Shirai, Yuichi Hashimoto, Shigeo Iwasaki, Kouzou Kaibuchi, Yasunori Kanaho, Toshiyuki Shirai, Yoh Terada, Koutarou Kimura, Satoshi Nagata, Yasuhisa Fukui

Research output: Contribution to journalArticlepeer-review

81 Citations (Scopus)

Abstract

We have purified a protein that binds phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] using beads bearing a PtdIns(3,4,5)P3 analogue. This protein, with a molecular mass of 43 kDa, was termed PtdIns(3,4,5)P3-binding protein. The partial amino acid sequences were determined and a full-length cDNA encoding the protein was isolated from bovine brain cDNA library. The clone harbored an open reading frame of 373 amino acids which contained one zinc finger motif similar to that of ADP-ribosylation-factor GTPase-activating protein and two pleckstrin homology domains. The entire sequence was 83% similar to centaurin α, another PtdIns(3,4,5)P3-binding protein. This protein bound PtdIns(3,4,5)P3 with a higher affinity than it did inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4-bisphosphate, and phosphatidylinositol 3-phosphate suggesting that the binding to PtdIns(3,4,5)P, was specific. The binding activity was weaker in the mutants with a point mutation in the conserved sequences in each pleckstrin homology domain. Introduction of both mutations abolished the activity. These results suggest that this new binding protein binds PtdIns(3,4,5)P3 through two pleckstrin domains present in the molecule.

Original languageEnglish
Pages (from-to)512-519
Number of pages8
JournalEuropean Journal of Biochemistry
Volume245
Issue number2
DOIs
Publication statusPublished - 1997

All Science Journal Classification (ASJC) codes

  • Biochemistry

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