Detail Positive Regulation of Itk PH Domain Function by Soluble IP4   Oleh:  Huang, Yina H. ; Grasis, Juris A. ; Miller, Andrew T. ; Xu, Ruo ; Soonthornvacharin, Stephen ; Andreotti, Amy H. ; Tsoukas, Constantine D. ; Cooke, Michael P. ; Sauer, Karsten Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 316 no. 5826 (May 2007), page 886. Topik: Cell Biology Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.05 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel Pleckstrin homology (PH) domain-mediated protein recruitment to cellular membranes is of paramount importance for signal transduction. The recruitment of many PH domains is controlled through production and turnover of their membrane ligand, phosphatidylinositol 3,4,S-trisphosphate (PIP3). We show that phosphorylation of the second messenger inositol l,4,S-trisphosphate (lP3) into inositoll,3,4,S-tetrakisphosphate (lp 4) establishes another mode of PH domain regulation through a soluble ligand. At physiological concentrations, IP4 promoted PH domain binding to PIP3. In primary mouse CD4+CDS+ thymocytes, this was required for full activation of the protein tyrosine kinase Itk after T cell receptor engagement. Our data suggest that IP4 establishes a feedback loop of phospholipase C-yl activation through Itk that is essential for T cell development. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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