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. 2006;46(1):314-23.
doi: 10.1016/j.advenzreg.2006.01.009. Epub 2006 Jul 20.

The regulation and function of inositol 1,4,5-trisphosphate 3-kinases

Robin F Irvine  1 , Samantha M Lloyd-Burton, Jowie C H Yu, Andrew J Letcher, Michael J Schell
Affiliations

The regulation and function of inositol 1,4,5-trisphosphate 3-kinases

Robin F Irvine et al. Adv Enzyme Regul. 2006.
No abstract available

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Figures

Fig. 1
Fig. 1
Ins(1,4,5)P3 binding to IP3KA. This illustration is derived from the structure of IP3KA with Ins(1,4,5)P3 and ATP bound to it, as described by Gonzalez et al. (2004). On the left is the original structure, and on the right is exactly the same, but with the three-helices insert (IP lobe) that is unique to the Ins(1,4,5)P3 3-kinases (Gonzalez et al., 2004) removed. Thus, the structure on the right envisions how Ins(1,4,5)P3 might bind to an InsP3 multikinase (lacking these three helices) which could, therefore, enable a wider range of substrates binding, including PtdIns(4,5)P2 (Resnick et al., 2005).
Fig. 2
Fig. 2
Dynamic localization of Ins(1,4,5)P3 3-kinase A in postsynaptic spines. The figure shows IP3KA transfected into hippocampal neurones, and illustrates (A) before, (B) 2 min after, treatment with 100 μM glutamate, and (C) 20 min after removal of 100 μM glutamate and the addition of MK-801, an NMDA receptor antagonist. The reversible shift from the spines to the shaft induced by glutamate is plainly visible. See (Schell and Irvine, 2006) for all details.
Fig. 3
Fig. 3
Pathways of InsP6 synthesis. The figure depicts the two likely pathways for InsP6 synthesis in mammlian cells. One route, the upper pathway (Odom et al., 2000), is found in yeast, may exist in mammals and does not involve any Ins(1,4,5)P3 3-kinase activity. The lower route (Balla et al., 1989; Shears, 1989) has IP33K as an essential first step.
See this image and copyright information in PMC

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