Inositol phospholipid binding

Maroun, C.R. et al., A conserved inositol phospholipid binding site within the pleckstrin homology domain of the Gabl docking protein is required for epithelial morphogenesis, J. Biol Chem., 274,31719,1999. 

Figure 14-3. Signaling through protein kinase C (PKC). Activated phospholipase C cleaves the inositol phospholipid PIP2 to form both soluble (IP3) and membrane-associated (DAG) second messengers. DAG recruits PKC to the membrane, where binding of calcium ions to PKC fully activates it. To accomplish this, IP3 promotes a transient increase of intracellular concentration by binding to a receptor on the endoplasmic reticulum, which opens a channel allowing release of stored calcium ions. PIP2, phosphatidylinositol 4,5-bisphosphate DAG, diacylglycerol PLC, phospholipase C IP3, inositol trisphosphate.

Dynamin is a microtubule-associated GTP-binding protein. Dynamins are activated by proteinkinase C. They have a PH, a pleckstrin-homology domain and bind inositol phospholipids which aaivate the GTPase of dynamin. Dynamins are involved in microtubule assembly and vesicular traffic. 

Table 1 Recognition of inositol phospholipids by specific phosphoinositide-binding domains ...

FIGURE 2. Post-receptor events initiated by H2- and H,-receptor activation by histamine (HIS). Adenylate cyclase (AC) stimulation occurs directly via H2-receptor activation or possibly indirectly via a calmodulin-calmodulin binding protein complex. Membrane inositol phospholipid (IPL) hydrolysis to inositol trisphosphate (IP3) is triggered by phospholipase C (PC) activation following H,-receptor stimulation. 

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