Phosphoinositide binding domains: embracing 3-phosphate

Article Abstract:

A study was conducted to better understand the structures of phosphoinosite-binding proteins and to explain how these cellular proteins select the products of phosphoinositide 3-kinase (P13K) and phosphatidylinositol (Ptdlns)-3,4,5-P3 over other abundant phosphoinositides such as Ptdlns-3P and Ptdlns-3,4-P2. Results suggest that the crystal and solution structure of FYVE domains of phosphoinositides induces the P13K selection while the selection of products of Ptdlns-3,4,5-P3 is triggered by the crystal structure of the pleckstrin domain.

Protein binding

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Phosphatidylinositol (3,4,5)P(sub 3) interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins

Article Abstract:

Phosphatidylinositol (3,4,5)P(sub 3) (PtdIns(3,4,5)P(sub 3)) binds to the Src homology 2 domains of phosphoinositide 3-kinase (PI 3-kinase). This binding prevents the interaction of PI 3-kinase with tyrosine-phosphorylated proteins. Suppressing the formation of PtdIns(3,4,5,)P(sub 3) increases PI 3-kinase binding to phosphorylated proteins. PtdIns(3,4,5,)P(sub 3) also binds to pp60(super c-src).

Observations, Proteins, Cooperative binding (Biochemistry)

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Signal transduction and membrane traffic: the PITP/phosphoinositide connection

Article Abstract:

The phosphatidylinositol (PtdIns) transfer protein/phosphoinositide (PITP) hypothesis suggests that Golgi membranes maintain proper PtdIns/PtdCho balance via the CDP-choline pathway. PITP is suggested to be influence polyphosphoinositide synthesis and phosphoinositide kinases, two substrates that play major roles in membrane transport by influencing the proteins that regulate vesicular traffic.

Cellular signal transduction

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