Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Positive regulation of ltk ph domain function by soluble ip(4)

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Huang, Y. H.
  • Grasis, J. A.
  • Miller, A. T.
  • Xu, R.
  • Soonthornvacharin, S.
  • Andreotti, A. H.
  • Tsoukas, C. D.
  • Cooke, M. P.
  • Sauer, Karsten

publication date

  • May 2007

journal

  • Science  Journal

abstract

  • 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 3,4,5-trisphosphate (PIP3). We show that phosphorylation of the second messenger inositol 1,4,5-trisphosphate (IP3) into inositol 1,3,4,5-tetrakisphosphate (IP4) 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+CD8+ 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-gamma1 activation through Itk that is essential for T cell development.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Motifs
  • Animals
  • Diglycerides
  • Feedback, Physiological
  • Inositol 1,4,5-Trisphosphate
  • Inositol Phosphates
  • Lymphopoiesis
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • Models, Biological
  • Organ Culture Techniques
  • Phosphatidylinositol Phosphates
  • Phospholipase C gamma
  • Phosphoproteins
  • Phosphorylation
  • Protein Structure, Tertiary
  • Protein-Tyrosine Kinases
  • Receptors, Antigen, T-Cell
  • Second Messenger Systems
  • Signal Transduction
  • Solubility
  • T-Lymphocytes
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1138684

PubMed ID

  • 17412921
scroll to property group menus

Additional Document Info

start page

  • 886

end page

  • 889

volume

  • 316

issue

  • 5826

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support