Pleckstrin homology domain as an inositol compound binding module

Masato Hirata, Takashi Kanematsu, Hiroshi Takeuchi, Hitoshi Yagisawa

研究成果: ジャーナルへの寄稿評論記事

31 引用 (Scopus)

抄録

Many of the proteins that participate in cell signalling contain structural modules involved in regulatory interactions between components of signal transduction cascades. One of such modules is the pleckstrin homology (PH) domain, a region of approximately 120 amino acids that can form an electrostatically polarized tertiary structure. Several molecules such as inositol 1,4,5-trisphosphate/phosphatidylinositol 4,5-bisphosphate, the βγ-subunits of heterotrimeric G proteins and protein kinase C have been proposed as common ligands for the PH domain. Through these potential interactions, the PH domain has been proposed to play a role in membrane recruitment of proteins containing the PH domain, thus targeting them to appropriate cellular compartment or enabling them to interact with other components of the signal transduction pathway. In this review, we mainly focus on membrane targeting through the binding to inositol phosphates/phosphoinositides.

元の言語英語
ページ(範囲)255-263
ページ数9
ジャーナルJapanese Journal of Pharmacology
76
発行部数3
DOI
出版物ステータス出版済み - 3 1 1998

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Inositol
Phosphatidylinositols
Signal Transduction
Heterotrimeric GTP-Binding Proteins
Inositol 1,4,5-Trisphosphate
Inositol Phosphates
Protein Kinase C
Membrane Proteins
Ligands
Amino Acids
Membranes
Pleckstrin Homology Domains
Proteins

All Science Journal Classification (ASJC) codes

  • Pharmacology

これを引用

Pleckstrin homology domain as an inositol compound binding module. / Hirata, Masato; Kanematsu, Takashi; Takeuchi, Hiroshi; Yagisawa, Hitoshi.

:: Japanese Journal of Pharmacology, 巻 76, 番号 3, 01.03.1998, p. 255-263.

研究成果: ジャーナルへの寄稿評論記事

Hirata, Masato ; Kanematsu, Takashi ; Takeuchi, Hiroshi ; Yagisawa, Hitoshi. / Pleckstrin homology domain as an inositol compound binding module. :: Japanese Journal of Pharmacology. 1998 ; 巻 76, 番号 3. pp. 255-263.
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